DB code: M00135

RLCP classification 3.103.90021.1120 : Transfer
CATH domain -.-.-.- :
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1
3.30.70.270 : Alpha-Beta Plaits Catalytic domain
3.30.70.270 : Alpha-Beta Plaits
3.30.70.270 : Alpha-Beta Plaits
3.30.420.10 : Nucleotidyltransferase; domain 5 Catalytic domain
-.-.-.- :
3.30.420.10 : Nucleotidyltransferase; domain 5 Catalytic domain
2.30.30.10 : SH3 type barrels.
-.-.-.- :
E.C. 3.4.23.- 2.7.7.49 3.1.26.4
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.30.30.10 : SH3 type barrels. M00206 M00146
3.10.10.10 : HIV Type 1 Reverse Transcriptase; Chain A, domain 1 M00206 M00146 M00166
3.30.420.10 : Nucleotidyltransferase; domain 5 M00206 T00252 M00019 M00020 M00055 M00146 M00166 M00173 M00175 M00186
3.30.70.270 : Alpha-Beta Plaits M00206 M00019 M00146 M00166 M00209

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains RefSeq MEROPS Pfam
P03355 Gag-Pol polyprotein
Pr180gag-pol
Matrix protein p15
(MA)
RNA-binding phosphoprotein p12 pp12
Capsid protein p30
(CA)
Nucleocapsid protein p10
(NC-pol)
Protease p14
(PR)
EC 3.4.23.-
Reverse transcriptase/ribonuclease H p80
(RT)
EC 2.7.7.49
EC 2.7.7.7
EC 3.1.26.4
Integrase p46
(IN)
NP_057933.2 (Protein)
NC_001501.1 (DNA/RNA sequence)
A02.008 (Aspartic)
PF01140 (Gag_MA)
PF01141 (Gag_p12)
PF02093 (Gag_p30)
PF00075 (RNase_H)
PF00665 (rve)
PF00077 (RVP)
PF00078 (RVT_1)
[Graphical View]

KEGG enzyme name
RNA-directed DNA polymerase
(EC 2.7.7.49 )
DNA nucleotidyltransferase (RNA-directed)
(EC 2.7.7.49 )
reverse transcriptase
(EC 2.7.7.49 )
revertase
(EC 2.7.7.49 )
RNA-dependent deoxyribonucleate nucleotidyltransferase
(EC 2.7.7.49 )
RNA revertase
(EC 2.7.7.49 )
RNA-dependent DNA polymerase
(EC 2.7.7.49 )
RNA-instructed DNA polymerase
(EC 2.7.7.49 )
RT
(EC 2.7.7.49 )
calf thymus ribonuclease H
(EC 3.1.26.4 )
endoribonuclease H (calf thymus)
(EC 3.1.26.4 )
RNase H
(EC 3.1.26.4 )
RNA*DNA hybrid ribonucleotidohydrolase
(EC 3.1.26.4 )
hybrid ribonuclease
(EC 3.1.26.4 )
hybridase
(EC 3.1.26.4 )
hybridase (ribonuclease H)
(EC 3.1.26.4 )
ribonuclease H
(EC 3.1.26.4 )
hybrid nuclease
(EC 3.1.26.4 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P03355 POL_MLVMO Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Endonucleolytic cleavage to 5''- phosphomonoester.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C02148 C00677 C00039 C00046 C00001 C00013 C00039 C00960
E.C. 2.7.7.49
2.7.7.49
3.1.26.4
3.1.26.4
2.7.7.49
2.7.7.49
3.1.26.4
Compound Divalent metal Deoxynucleoside triphosphate DNA(n) RNA H2O Pyrophosphate DNA(n+1) RNA 5'-phosphate
Type divalent metal (Ca2+, Mg2+) nucleotide nucleic acids nucleic acids H2O phosphate group/phosphate ion nucleic acids nucleic acids,phosphate group/phosphate ion
ChEBI 15377
29888
PubChem 22247451
962
1023
21961011
1d0eA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:T-T-T-C-A-T-G-C-A-T-G (chain E), T-T-T-C-A-T-G-C-A-T-G (chain F) Unbound Unbound Unbound Unbound
1d0eB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d1uA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-C-G-T-G (chain B), A-C-G-G-C-A-C-G-A-G (chain C) Unbound Unbound Unbound Unbound
1mmlA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1n4lA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-T-T-T-T-A-A-A-A-G-A-A-A-A-G (chain B), C-T-T-T-T-C-T-T-T-T-A-A-A-A-A-G (chain D) Unbound Unbound Unbound Unbound
1nndA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qaiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-A-T-G-C-A-T-G (chain D) Unbound Unbound Unbound Unbound
1qaiB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-A-T-G-C-A-T-G (chain C) Unbound Unbound Unbound Unbound
1qajA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-A-T-G-C-A-T-G (chain C), C-A-T-G-C-A-T-G (chain D) Unbound Unbound Unbound Unbound
1qajB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1i6jA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:G-T-C-G-T-C (chain B), A-C-G-G-G-A-C-G-A-C (chain C) Unbound Unbound Unbound Unbound
1zttA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-T-A-A-T-T-C (chain B), G-A-A-T-T-A-A-G (chain G) Unbound Unbound Unbound Unbound
1ztwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-T-A-A-T-T-C (chain B), G-A-A-T-T-A-A-G (chain G) Unbound Unbound Unbound Unbound
2fjvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-T-A-A-T-T-C (chain B), G-A-A-T-T-A-A-G (chain G) Unbound Unbound Unbound Unbound
2fjwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-T-G-A-A-T-G (chain B), C-A-T-T-C-A-A-G (chain G) Unbound Unbound Unbound Unbound
2fjxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:C-T-T-G-A-A-T-G (chain B), C-A-T-T-C-A-A-G (chain G) Unbound Unbound Unbound Unbound
1rw3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d0eA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d0eB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d1uA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mmlA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1n4lA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1nndA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qaiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qaiB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qajA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qajB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1i6jA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1zttA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ztwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2fjvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2fjwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2fjxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1rw3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1rw3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1rw3A04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2], [3], [18]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1d0eA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1d0eB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1d1uA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mmlA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1n4lA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1nndA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant R116A
1qaiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qaiB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qajA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qajB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1i6jA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1zttA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ztwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2fjvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2fjwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2fjxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1rw3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1d0eA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1d0eB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1d1uA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1mmlA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1n4lA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1nndA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1qaiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1qaiB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1qajA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1qajB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1i6jA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1zttA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1ztwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
2fjvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
2fjwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
2fjxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1rw3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 150;ASP 224;ASP 225(Divalent metals binding) ASP 153;ALA 154
1rw3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1rw3A04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.5, p.35-36
[3]
p.884-888
[4]
Fig.7, p.5359
[18]
Fig.1, p.14839-14841
[20]
p.824-826

References
[1]
Resource
Comments
Medline ID
PubMed ID 1370551
Journal J Virol
Year 1992
Volume 66
Pages 615-22
Authors Telesnitsky A, Blain SW, Goff SP
Title Defects in Moloney murine leukemia virus replication caused by a reverse transcriptase mutation modeled on the structure of Escherichia coli RNase H.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 130-394.
Medline ID 96097395
PubMed ID 8535782
Journal Structure
Year 1995
Volume 3
Pages 879-92
Authors Georgiadis MM, Jessen SM, Ogata CM, Telesnitsky A, Goff SP, Hendrickson WA
Title Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase.
Related PDB 1mml
Related UniProtKB P03355
[4]
Resource
Comments
Medline ID
PubMed ID 7537090
Journal Biochemistry
Year 1995
Volume 34
Pages 5351-63
Authors Patel PH, Jacobo-Molina A, Ding J, Tantillo C, Clark AD Jr, Raag R, Nanni RG, Hughes SH, Arnold E
Title Insights into DNA polymerization mechanisms from structure and function analysis of HIV-1 reverse transcriptase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9684890
Journal Protein Sci
Year 1998
Volume 7
Pages 1575-82
Authors Sun D, Jessen S, Liu C, Liu X, Najmudin S, Georgiadis MM
Title Cloning, expression, and purification of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase: crystallization of nucleic acid complexes.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9741851
Journal Proteins
Year 1998
Volume 33
Pages 135-43
Authors Goedken ER, Marqusee S
Title Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10600369
Journal J Mol Biol
Year 1999
Volume 294
Pages 1097-113
Authors Gao HQ, Sarafianos SG, Arnold E, Hughes SH
Title Similarities and differences in the RNase H activities of human immunodeficiency virus type 1 reverse transcriptase and Moloney murine leukemia virus reverse transcriptase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10957631
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 1120-31
Authors Cote ML, Yohannan SJ, Georgiadis MM
Title Use of an N-terminal fragment from moloney murine leukemia virus reverse transcriptase to facilitate crystallization and analysis of a pseudo-16-mer DNA molecule containing G-A mispairs.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10913435
Journal J Biol Chem
Year 2000
Volume 275
Pages 32299-309
Authors Schultz SJ, Zhang M, Kelleher CD, Champoux JJ
Title Analysis of plus-strand primer selection, removal, and reutilization by retroviral reverse transcriptases.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10669612
Journal J Mol Biol
Year 2000
Volume 296
Pages 613-32
Authors Najmudin S, Cote ML, Sun D, Yohannan S, Montano SP, Gu J, Georgiadis MM
Title Crystal structures of an N-terminal fragment from Moloney murine leukemia virus reverse transcriptase complexed with nucleic acid: functional implications for template-primer binding to the fingers domain.
Related PDB 1d0e 1qai 1qaj
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11000235
Journal J Virol
Year 2000
Volume 74
Pages 9629-36
Authors Pfeiffer JK, Georgiadis MM, Telesnitsky A
Title Structure-based moloney murine leukemia virus reverse transcriptase mutants with altered intracellular direct-repeat deletion frequencies.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10888659
Journal J Virol
Year 2000
Volume 74
Pages 7171-8
Authors Svarovskaia ES, Delviks KA, Hwang CK, Pathak VK
Title Structural determinants of murine leukemia virus reverse transcriptase that affect the frequency of template switching.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11526315
Journal Acta Crystallogr D Biol Crystallogr
Year 2001
Volume 57
Pages 1238-50
Authors Cote ML, Georgiadis MM
Title Structure of a pseudo-16-mer DNA with stacked guanines and two G-A mispairs complexed with the N-terminal fragment of Moloney murine leukemia virus reverse transcriptase.
Related PDB 1i6j
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11124910
Journal J Mol Biol
Year 2001
Volume 305
Pages 341-59
Authors Gu J, Villanueva RA, Snyder CS, Roth MJ, Georgiadis MM
Title Substitution of Asp114 or Arg116 in the fingers domain of moloney murine leukemia virus reverse transcriptase affects interactions with the template-primer resulting in decreased processivity.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11259203
Journal Virology
Year 2001
Volume 282
Pages 206-13
Authors Boyer PL, Gao HQ, Frank P, Clark PK, Hughes SH
Title The basic loop of the RNase H domain of MLV RT is important both for RNase H and for polymerase activity.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11237609
Journal J Mol Biol
Year 2001
Volume 306
Pages 931-43
Authors Winshell J, Champoux JJ
Title Structural alterations in the DNA ahead of the primer terminus during displacement synthesis by reverse transcriptases.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 11433017
Journal Nucleic Acids Res
Year 2001
Volume 29
Pages 2725-32
Authors Berthet N, Roupioz Y, Constant JF, Kotera M, Lhomme J
Title Translesional synthesis on DNA templates containing the 2'-deoxyribonolactone lesion.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 12475231
Journal Biochemistry
Year 2002
Volume 41
Pages 14831-42
Authors Shi Q, Singh K, Srivastava A, Kaushik N, Modak MJ
Title Lysine 152 of MuLV reverse transcriptase is required for the integrity of the active site.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12818202
Journal J Mol Biol
Year 2003
Volume 330
Pages 57-74
Authors Cote ML, Pflomm M, Georgiadis MM
Title Staying straight with A-tracts: a DNA analog of the HIV-1 polypurine tract.
Related PDB 1n4l
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 15130474
Journal Structure
Year 2004
Volume 12
Pages 819-29
Authors Das D, Georgiadis MM
Title The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus.
Related PDB 1rw3
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 16049022
Journal Nucleic Acids Res
Year 2005
Volume 33
Pages 4106-16
Authors Goodwin KD, Long EC, Georgiadis MM
Title A host-guest approach for determining drug-DNA interactions: an example using netropsin.
Related PDB 1ztt 1ztw
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 16771498
Journal J Am Chem Soc
Year 2006
Volume 128
Pages 7846-54
Authors Goodwin KD, Lewis MA, Tanious FA, Tidwell RR, Wilson WD, Georgiadis MM, Long EC
Title A high-throughput, high-resolution strategy for the study of site-selective DNA binding agents: Analysis of a "highly twisted" benzimidazole-diamidine.
Related PDB 2fjv 2fjw 2fjx
Related UniProtKB

Comments
This enzyme is composed of the N-terminal protease domain (EC 3.4.23.-), reverse transcriptase domain (E.C. 2.7.7.49), RNase H domain (3.1.26.4), and integrase domain. Only the catalytic domain of the reverse transcriptase (2.7.7.49) has been solved so far.
According to the literature [2], [3], [18], the reaction of reverse transcriptase seems to proceed as follows:
(1) 3'-hydroxyl group of DNA is activated by a magnesium ion, which is bound to Asp150 and Asp224.
(2) The activated 3'-hydroxyl group makes a nucleophilic attack on the alpha-phosphoryl group of dNTP, forming pentacovalent transition state.
(3) The transition state is stabilized by both the two magnesium ions.
(4) Stabilization by the second magnesium ion and the mainchain amide groups of Asp153 and Ala154 facilitate the leaving of beta- and gamma-phosphate groups.

Created Updated
2003-07-31 2009-02-26