EzCatDB: M00217
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DB codeM00217
RLCP classification1.13.30000.41 : Hydrolysis
1.13.30000.42 : Hydrolysis
CATH domainDomain 14.10.80.- : Rhinovirus 14, subunit 4
Domain 22.60.120.- : Jelly Rolls
Domain 32.60.120.- : Jelly Rolls
Domain 42.60.120.- : Jelly Rolls
Domain 52.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 62.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 7-.-.-.-
Domain 8-.-.-.-
Domain 91.-.-.-
Domain 10-.-.-.-
Domain 112.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 122.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 133.-.-.-
Domain 143.30.70.- : Alpha-Beta Plaits
Domain 151.20.960.- : Mitochondrial Import Receptor Subunit Tom20; Chain A
E.C.3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48
CSA1cqq

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P03300P04936P08292
Protein nameGenome polyproteinGenome polyproteinGenome polyproteinpicornain 2A
   (EC 3.4.22.29)

picornavirus endopeptidase 2A
   (EC 3.4.22.29)

poliovirus protease 2A
   (EC 3.4.22.29)

rhinovirus protease 2A
   (EC 3.4.22.29)

2A protease
   (EC 3.4.22.29)

2A proteinase
   (EC 3.4.22.29)

protease 2A
   (EC 3.4.22.29)

proteinase 2Apro
   (EC 3.4.22.29)

picornaviral 2A proteinase
   (EC 3.4.22.29)

Y-G proteinase 2A
   (EC 3.4.22.29)

poliovirus proteinase 2A
   (EC 3.4.22.29)

poliovirus protease 2Apro
   (EC 3.4.22.29)

picornaviral 2A proteinase
   (EC 3.4.22.29)

nucleoside-triphosphatase
   (EC 3.6.1.15)

nucleoside triphosphate phosphohydrolase
   (EC 3.6.1.15)

nucleoside-5-triphosphate phosphohydrolase
   (EC 3.6.1.15)

nucleoside 5-triphosphatase
   (EC 3.6.1.15)

picornain 3C
   (EC 3.4.22.28)

picornavirus endopeptidase 3C
   (EC 3.4.22.28)

poliovirus protease 3C
   (EC 3.4.22.28)

rhinovirus protease 3C
   (EC 3.4.22.28)

foot-and-mouth protease 3C
   (EC 3.4.22.28)

poliovirus proteinase 3C
   (EC 3.4.22.28)

rhinovirus proteinase 3C
   (EC 3.4.22.28)

coxsackievirus 3C proteinase
   (EC 3.4.22.28)

foot-and-mouth-disease virus proteinase 3C
   (EC 3.4.22.28)

3C protease
   (EC 3.4.22.28)

3C proteinase
   (EC 3.4.22.28)

cysteine proteinase 3C
   (EC 3.4.22.28)

hepatitis A virus 3C proteinase
   (EC 3.4.22.28)

protease 3C
   (EC 3.4.22.28)

tomato ringspot nepovirus 3C-related protease
   (EC 3.4.22.28)

RNA-directed RNA polymerase
   (EC 2.7.7.48)

RNA nucleotidyltransferase (RNA-directed)
   (EC 2.7.7.48)

RNA nucleotidyltransferase (RNA-directed)
   (EC 2.7.7.48)

RNA-dependent ribonucleate nucleotidyltransferase
   (EC 2.7.7.48)

3D polymerase
   (EC 2.7.7.48)

PB1 proteins
   (EC 2.7.7.48)

PB2 proteins
   (EC 2.7.7.48)

phage f2 replicase
   (EC 2.7.7.48)

polymerase L
   (EC 2.7.7.48)

Q-beta replicase
   (EC 2.7.7.48)

phage f2 replicase
   (EC 2.7.7.48)

ribonucleic acid replicase
   (EC 2.7.7.48)

ribonucleic acid-dependent ribonucleate nucleotidyltransferase
   (EC 2.7.7.48)

ribonucleic acid-dependent ribonucleic acid polymerase
   (EC 2.7.7.48)

ribonucleic replicase
   (EC 2.7.7.48)

ribonucleic synthetase
   (EC 2.7.7.48)

RNA replicase
   (EC 2.7.7.48)

RNA synthetase
   (EC 2.7.7.48)

RNA transcriptase
   (EC 2.7.7.48)

RNA-dependent ribonucleate nucleotidyltransferase
   (EC 2.7.7.48)

RDRP
   (EC 2.7.7.48)

RNA-dependent RNA polymerase
   (EC 2.7.7.48)

RNA-dependent RNA replicase
   (EC 2.7.7.48)

transcriptase
   (EC 2.7.7.48)

SynonymsNoneNoneNone
ContainsProtein VP0 VP4-VP2
Protein VP4 Virion protein 4 P1A
Protein VP2 Virion protein 2 P1B
Protein VP3 Virion protein 3 P1C
Protein VP1 Virion protein 1 P1D
Picornain 2A
(Protein 2A)
(P2A)
   EC 3.4.22.29
Protein 2B
(P2B)
Protein 2C
(P2C)
   EC 3.6.1.15
Protein 3A
(P3A)
Protein 3B
(P3B)
VPg
Picornain 3C
   EC 3.4.22.28
Protease 3C
(P3C)
RNA-directed RNA polymerase 3D-POL
(P3D-POL)
   EC 2.7.7.48
Protein VP0 VP4-VP2
Protein VP4 Virion protein 4 P1A
Protein VP2 Virion protein 2 P1B
Protein VP3 Virion protein 3 P1C
Protein VP1 Virion protein 1 P1D
Picornain 2A
(Protein 2A)
(P2A)
   EC 3.4.22.29
Protein 2B
(P2B)
Protein 2C
(P2C)
   EC 3.6.1.15
Protein 3A
(P3A)
Protein 3B
(P3B)
VPg
Picornain 3C
   EC 3.4.22.28
Protease 3C
(P3C)
RNA-directed RNA polymerase 3D-POL
(P3D-POL)
   EC 2.7.7.48
Protein VP0 VP4-VP2
Protein VP4 Virion protein 4 P1A
Protein VP2 Virion protein 2 P1B
Protein VP3 Virion protein 3 P1C
Protein VP1 Virion protein 1 P1D
Picornain 2A
(Protein 2A)
(P2A)
   EC 3.4.22.29
Protein 2B
(P2B)
Protein 2C
(P2C)
   EC 3.6.1.15
Protein 3A
(P3A)
Protein 3B
(P3B)
VPg
Picornain 3C
   EC 3.4.22.28
Protease 3C
(P3C)
RNA-directed RNA polymerase 3D-POL
(P3D-POL)
   EC 2.7.7.48
RefSeqNP_041277.1 (Protein)
NC_002058.3 (DNA/RNA sequence)


MEROPSC03.001 (Cysteine)
C03.021 (Cysteine)
C03.011 (Cysteine)
PfamPF08727 (P3A)
PF00548 (Peptidase_C3)
PF02226 (Pico_P1A)
PF00947 (Pico_P2A)
PF01552 (Pico_P2B)
PF00680 (RdRP_1)
PF00073 (Rhv)
PF00910 (RNA_helicase)
[Graphical view]
PF08727 (P3A)
PF00548 (Peptidase_C3)
PF02226 (Pico_P1A)
PF00947 (Pico_P2A)
PF01552 (Pico_P2B)
PF00680 (RdRP_1)
PF00073 (Rhv)
PF00910 (RNA_helicase)
[Graphical view]
PF08727 (P3A)
PF00548 (Peptidase_C3)
PF02226 (Pico_P1A)
PF00947 (Pico_P2A)
PF01552 (Pico_P2B)
PF00680 (RdRP_1)
PF00073 (Rhv)
PF00910 (RNA_helicase)
[Graphical view]

KEGG pathways
MAP codePathwaysE.C.
MAP00230Purine metabolism3.6.1.15,2.7.7.48
MAP00730Thiamine metabolism3.6.1.15

UniProtKB:Accession NumberP03300P04936P08292
Entry namePOLG_POL1MPOLG_HRV2POLG_CXB4J
ActivityNucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).,Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.,Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.,NTP + H(2)O = NDP + phosphate.Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).,Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.,Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.,NTP + H(2)O = NDP + phosphate.Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).,Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.,Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.,NTP + H(2)O = NDP + phosphate.
SubunitP2C N-terminus interacts with human RTN3. This interaction is important for viral replication (By similarity). Interacts with human PVR.Capsid proteins interact with host ICAM1 (By similarity).Capsid proteins interact with host CXADR.
Subcellular locationProtein VP2: Virion. Cytoplasm (Potential).,Protein VP3: Virion. Cytoplasm (Potential).,Protein VP1: Virion. Cytoplasm (Potential).,Protein 2B: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 2C: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 3A: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 3B: Virion (Potential).,Picornain 3C: Cytoplasm (Potential).,RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).Protein VP2: Virion. Cytoplasm (Potential).,Protein VP3: Virion. Cytoplasm (Potential).,Protein VP1: Virion. Cytoplasm (Potential).,Protein 2B: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 2C: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 3A: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 3B: Virion (Potential).,Picornain 3C: Cytoplasm (Potential).,RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).Protein VP2: Virion. Cytoplasm (Potential).,Protein VP3: Virion. Cytoplasm (Potential).,Protein VP1: Virion. Cytoplasm (Potential).,Protein 2B: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 2C: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 3A: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).,Protein 3B: Virion (Potential).,Picornain 3C: Cytoplasm (Potential).,RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
Cofactor



Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00038C00305C00017C00001C00201C00046C00017C00012C00454C00009C00046C00013I00153I00154I00155
E.C.3.4.22.292.7.7.483.4.22.28,3.4.22.293.4.22.28,3.4.22.29,3.6.1.153.6.1.15,2.7.7.482.7.7.483.4.22.28,3.4.22.293.4.22.28,3.4.22.293.6.1.153.6.1.152.7.7.482.7.7.483.4.22.283.4.22.283.4.22.28
CompoundZincMagnesiumProteinH2ONucleoside triphosphateRNA(n)ProteinPeptideNucleoside diphosphatePhosphateRNA(n+1)DiphosphatePeptidyl-Cys-tetrahedral-intermediate (with previous peptide)Acyl-enzyme(Peptidyl-Cys-acyl group)Peptidyl-Cys-tetrahedral-intermediate
Typeheavy metaldivalent metal (Ca2+, Mg2+)peptide/proteinH2Onucleotidenucleic acidspeptide/proteinpeptide/proteinnucleotidephosphate group/phosphate ionnucleic acidsphosphate group/phosphate ion


ChEBI29105
18420

15377





26078

29888



PubChem32051
888

962
22247451





22486802
1004

21961011
1023



                       
2hrvA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2hrvB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1z8rA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2hrvA02Bound:_ZNUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2hrvB02Bound:_ZNUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1z8rA02Bound:_ZNUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l1nA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l1nB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cqqA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l1nA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l1nB02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cqqA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:AG7UnboundUnbound

Active-site residues
resource
Swiss-prot;P03300, P04936 & literature [7], [11]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
            
2hrvA01HIS 18;ASP 35
 
 
 
2hrvB01HIS 18;ASP 35
 
 
 
1z8rA01HIS 21;ASP 39
 
 
 
2hrvA02CYS 106
CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding)
GLY 104;CYS 106
 
2hrvB02CYS 106
CYS 52;CYS 54;CYS 112;HIS 114(Zinc binding)
GLY 104;CYS 106
 
1z8rA02       
CYS 56;CYS 58;CYS 116;HIS 118(Zinc binding)
GLY 108;       
mutant C110A
1l1nA01HIS 40;GLU 71
 
 
 
1l1nB01HIS 40;GLU 71
 
 
 
1cqqA01HIS 40;GLU 71
 
 
 
1l1nA02CYS 147
 
GLY 145;CYS 147
 
1l1nB02CYS 147
 
GLY 145;CYS 147
 
1cqqA02CYS 147
 
GLY 145;CYS 147
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.110
[4]p.623-624
[9]p.763-765, p.767-769
[12]p.1440-1441
[17]p.210
[19]p.11000-11001
[21]p.5468-5469
[30]


references
[1]
PubMed ID3186696
JournalProc Natl Acad Sci U S A
Year1988
Volume85
Pages7872-6
AuthorsBazan JF, Fletterick RJ
TitleViral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications.
[2]
PubMed ID2645167
JournalFEBS Lett
Year1989
Volume243
Pages103-14
AuthorsGorbalenya AE, Donchenko AP, Blinov VM, Koonin EV
TitleCysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold.
[3]
PubMed ID1849679
JournalVirology
Year1991
Volume181
Pages609-19
AuthorsKean KM, Teterina NL, Marc D, Girard M
TitleAnalysis of putative active site residues of the poliovirus 3C protease.
[4]
PubMed ID1850921
JournalVirology
Year1991
Volume182
Pages615-25
AuthorsYu SF, Lloyd RE
TitleIdentification of essential amino acid residues in the functional activity of poliovirus 2A protease.
[5]
PubMed ID1331062
JournalJ Biol Chem
Year1992
Volume267
Pages22639-44
AuthorsSommergruber W, Ahorn H, Zophel A, Maurer-Fogy I, Fessl F, Schnorrenberg G, Liebig HD, Blaas D, Kuechler E, Skern T
TitleCleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A.
[6]
PubMed ID8320292
JournalJ Chem Inf Comput Sci
Year1993
Volume33
Pages345-9
AuthorsArad D, Kreisberg R, Shokhen M
TitleStructural and mechanistic aspects of 3C proteases from the Picornavirus family.
[7]
PubMed ID8386363
JournalProtein Eng
Year1993
Volume6
Pages189-93
AuthorsMiyashita K, Kusumi M, Utsumi R, Katayama S, Noda M, Komano T, Satoh N
TitleSite-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: evidence of a functional relationship with trypsin-like serine proteinases.
[8]
PubMed ID8097606
JournalVirology
Year1993
Volume194
Pages360-4
AuthorsKean KM, Howell MT, Grunert S, Girard M, Jackson RJ
TitleSubstitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites.
[9]
PubMed ID7515772
JournalCell
Year1994
Volume77
Pages761-71
AuthorsMatthews DA, Smith WW, Ferre RA, Condon B, Budahazi G, Sisson W, Villafranca JE, Janson CA, McElroy HE, Gribskov CL, et al
TitleStructure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein.
[10]
PubMed ID8164744
JournalNature
Year1994
Volume369
Pages72-6
AuthorsAllaire M, Chernaia MM, Malcolm BA, James MN
TitlePicornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.
[11]
PubMed ID8112306
JournalEMBO J
Year1994
Volume13
Pages924-7
AuthorsMacadam AJ, Ferguson G, Fleming T, Stone DM, Almond JW, Minor PD
TitleRole for poliovirus protease 2A in cap independent translation.
[12]
PubMed ID8520469
JournalProtein Sci
Year1995
Volume4
Pages1439-45
AuthorsMalcolm BA
TitleThe picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.
[13]
PubMed ID8580843
JournalProtein Sci
Year1995
Volume4
Pages2526-31
AuthorsVoss T, Meyer R, Sommergruber W
TitleSpectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity.
[14]
PubMed ID8615011
JournalVirology
Year1996
Volume218
Pages1-13
AuthorsBlair WS, Nguyen JH, Parsley TB, Semler BL
TitleMutations in the poliovirus 3CD proteinase S1-specificity pocket affect substrate recognition and RNA binding.
[15]
CommentsX-ray crystallography
PubMed ID9367789
JournalJ Mol Biol
Year1997
Volume273
Pages1032-47
AuthorsMosimann SC, Cherney MM, Sia S, Plotch S, James MN
TitleRefined X-ray crystallographic structure of the poliovirus 3C gene product.
Related PDB1l1n
[16]
PubMed ID9139725
JournalJ Biol Chem
Year1997
Volume272
Pages12683-91
AuthorsBarco A, Ventoso I, Carrasco L
TitleThe yeast Saccharomyces cerevisiae as a genetic system for obtaining variants of poliovirus protease 2A.
[17]
PubMed ID9268151
JournalVirology
Year1997
Volume234
Pages203-14
AuthorsSommergruber W, Seipelt J, Fessl F, Skern T, Liebig HD, Casari G
TitleMutational analyses support a model for the HRV2 2A proteinase.
[18]
PubMed ID10400760
JournalJ Virol
Year1999
Volume73
Pages6626-33
AuthorsSosnovtseva SA, Sosnovtsev SV, Green KY
TitleMapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.
[19]
CommentsX-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1507-1686.
PubMed ID10500114
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages11000-7
AuthorsMatthews DA, Dragovich PS, Webber SE, Fuhrman SA, Patick AK, Zalman LS, Hendrickson TF, Love RA, Prins TJ, Marakovits JT, Zhou R, Tikhe J, Ford CE, Meador JW, Ferre RA, Brown EL, Binford SL, Brothers MA, DeLisle DM, Worland ST
TitleStructure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.
Related PDB1cqq
Related UniProtKBP04936
[20]
PubMed ID10507325
JournalVirus Res
Year1999
Volume62
Pages159-68
AuthorsSeipelt J, Guarne A, Bergmann E, James M, Sommergruber W, Fita I, Skern T
TitleThe structures of picornaviral proteinases.
[21]
CommentsX-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 850-991.
PubMed ID10523291
JournalEMBO J
Year1999
Volume18
Pages5463-75
AuthorsPetersen JF, Cherney MM, Liebig HD, Skern T, Kuechler E, James MN
TitleThe structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis.
Related PDB2hrv
Related UniProtKBP04936
[22]
PubMed ID11056105
JournalCirculation
Year2000
Volume102
Pages2276-81
AuthorsBadorff C, Fichtlscherer B, Rhoads RE, Zeiher AM, Muelsch A, Dimmeler S, Knowlton KU
TitleNitric oxide inhibits dystrophin proteolysis by coxsackieviral protease 2A through S-nitrosylation: A protective mechanism against enteroviral cardiomyopathy.
[23]
PubMed ID11007981
JournalFEBS Lett
Year2000
Volume481
Pages289-92
AuthorsSarkany Z, Skern T, Polgar L
TitleCharacterization of the active site thiol group of rhinovirus 2A proteinase.
[24]
PubMed ID10769080
JournalJ Gen Virol
Year2000
Volume81
Pages1361-72
AuthorsSantti J, Harvala H, Kinnunen L, Hyypia T
TitleMolecular epidemiology and evolution of coxsackievirus A9.
[25]
PubMed ID11162821
JournalVirology
Year2001
Volume280
Pages80-6
AuthorsWang QM, Johnson RB
TitleActivation of human rhinovirus-14 3C protease.
[26]
PubMed ID11161279
JournalJ Gen Virol
Year2001
Volume82
Pages397-408
AuthorsLi X, Lu HH, Mueller S, Wimmer E
TitleThe C-terminal residues of poliovirus proteinase 2A(pro) are critical for viral RNA replication but not for cis- or trans-proteolytic cleavage.
[27]
PubMed ID12525179
JournalBiochemistry
Year2003
Volume42
Pages516-22
AuthorsSarkany Z, Polgar L
TitleThe unusual catalytic triad of poliovirus protease 3C.
[28]
PubMed ID14966374
JournalJ Biomed Sci
Year2004
Volume11
Pages239-48
AuthorsShih SR, Chiang C, Chen TC, Wu CN, Hsu JT, Lee JC, Hwang MJ, Li ML, Chen GW, Ho MS
TitleMutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activities.
[29]
PubMed ID16227288
JournalJ Virol
Year2005
Volume79
Pages13685-93
AuthorsNakamura K, Someya Y, Kumasaka T, Ueno G, Yamamoto M, Sato T, Takeda N, Miyamura T, Tanaka N
TitleA norovirus protease structure provides insights into active and substrate binding site integrity.
[30]
CommentsX-ray crystallography
PubMed ID16415022
JournalJ Virol
Year2006
Volume80
Pages1451-62
AuthorsBaxter NJ, Roetzer A, Liebig HD, Sedelnikova SE, Hounslow AM, Skern T, Waltho JP
TitleStructure and dynamics of coxsackievirus B4 2A proteinase, an enyzme involved in the etiology of heart disease.
Related PDB1z8r

comments
This protein is a genome polyprotein from picornavirus, which is composed of 4 coat proteins, 3 core proteins, 2 proteases (picornain 2A, picornain 3C), genome-linked protein, 3D polymerase.
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One of the protease enzymes in this entry is picornain 2A (E.C. 3.4.22.29), which cleaves TYR-|-GLY bond in virus polyprotein.
Although zinc is included as cofactor, it is not involved in catalysis (see [13], [21]).
This enzyme belongs to the peptidase family-C3, to which the other protease, picornain 3C (E.C. 3.4.22.28;M00209, M00216 in EzCatDB, and described below) belongs.
The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), which is its homologous enzyme, although its catalytic site is composed of Cys/His/Asp and mainchain amide groups.
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The other protease enzyme in this entry is picornain 3C (EC 3.4.22.28) from poliovirus or rhinovirus, whitch cleaves GLN/GLU-|-GLY/SER/THR bonds in its polyprotein.
This enzyme belongs to the peptidase family-C3, to which picornain 3C from other viruses (M00209, M00216 in EzCatDB) and picornain 2A (EC 3.4.22.29; described above) belong.
The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), which is its homologous enzyme, although its catalytic site is composed of Cys/His/Glu and mainchain amide groups.

createdupdated
2006-07-212012-10-22


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