DB code: D00169

RLCP classification 1.30.36010.970 : Hydrolysis
CATH domain 2.80.10.50 : Trefoil (Acidic Fibroblast Growth Factor, subunit A)
3.20.20.80 : TIM Barrel Catalytic domain
E.C. 3.2.1.8
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.20.20.80 : TIM Barrel S00202 S00210 S00748 S00906 S00907 S00911 S00912 S00915 M00134 M00160 D00479 S00204 S00205 S00206 S00207 S00203 S00208 S00209 S00211 S00213 S00214 M00113 T00307 D00165 D00166 D00176 D00501 D00502 D00503 D00844 D00861 D00864 M00026 M00112 M00193 M00346 T00057 T00062 T00063 T00066 T00067
2.80.10.50 : Trefoil (Acidic Fibroblast Growth Factor, subunit A) D00666 M00185

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P26514 Endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase A
CBM13 (Carbohydrate-Binding Module Family 13)
GH10 (Glycoside Hydrolase Family 10)
PF00331 (Glyco_hydro_10)
PF00652 (Ricin_B_lectin)
[Graphical View]
Q7SI98
Hydrolase
CBM13 (Carbohydrate-Binding Module Family 13)
GH10 (Glycoside Hydrolase Family 10)
PF00331 (Glyco_hydro_10)
PF00652 (Ricin_B_lectin)
[Graphical View]

KEGG enzyme name
endo-1,4-beta-xylanase
endo-(1->4)-beta-xylan 4-xylanohydrolase
endo-1,4-xylanase
xylanase
beta-1,4-xylanase
endo-1,4-xylanase
endo-beta-1,4-xylanase
endo-1,4-beta-D-xylanase
1,4-beta-xylan xylanohydrolase
beta-xylanase
beta-1,4-xylan xylanohydrolase
endo-1,4-beta-xylanase
beta-D-xylanase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q7SI98 Q7SI98_STROI
P26514 XYNA_STRLI Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00707 C00001 C00707 C00707
E.C.
Compound Xylan H2O Xylan Xylan
Type polysaccharide H2O polysaccharide polysaccharide
ChEBI 15377
PubChem 22247451
962
1xyfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1xyfB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isvB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iswA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iswB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isxB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isyA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isyB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iszA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iszB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1it0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1it0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1knlA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1knmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1mc9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1xyfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1xyfB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isvB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iswA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:XYP-XYP(chain C) Bound:XYP-XYP(chain D) Unbound
1iswB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:XYP-XYP(chain F) Bound:XYP-XYP(chain G) Unbound
1isxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:XYP-XYP-XYP(chain C) Bound:XYP-XYP(chain D) Unbound
1isxB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:XYP-XYP-XYP(chain F) Bound:XYP-XYP-XYP(chain G) Unbound
1isyA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1isyB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iszA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1iszB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1it0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1it0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1e0vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-analogue:FFC
1e0wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1e0xA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-analogue:XYP-X2F
1e0xB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-analogue:XYP-X2F
1od8A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:XYP-XDL Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1xyf, Swiss-prot;P26514

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1xyfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1xyfB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1isvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1isvB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iswA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iswB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1isxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1isxB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1isyA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1isyB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iszA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iszB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1it0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1it0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1knlA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1knmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mc9A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1xyfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1xyfB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1isvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1isvB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1iswA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1iswB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1isxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1isxB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1isyA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1isyB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1iszA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1iszB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1it0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1it0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 628;HIS 707;GLU 736;ASP 738
1e0vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1e0wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1e0xA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1e0xB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238
1od8A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 128;HIS 207;GLU 236;ASP 238

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[7]
[11]
Fig.4
[12]
p.20813
[19]
[20]
[22]
Fig.1 4

References
[1]
Resource
Comments
Medline ID
PubMed ID 3141761
Journal Microbiol Rev
Year 1988
Volume 52
Pages 305-17
Authors Wong KK, Tan LU, Saddler JN
Title Multiplicity of beta-1,4-xylanase in microorganisms: functions and applications.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1368510
Journal Agric Biol Chem
Year 1990
Volume 54
Pages 449-57
Authors Yoshida S, Kusakabe I, Matsuo N, Shimizu K, Yasui T, Murakami K
Title Structure of rice-straw arabinoglucuronoxylan and specificity of Streptomyces xylanase toward the xylan.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1761039
Journal Eur J Biochem
Year 1991
Volume 202
Pages 367-77
Authors Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC Jr
Title Structural and functional relationships in two families of beta-1,4-glycanases.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1886523
Journal Microbiol Rev
Year 1991
Volume 55
Pages 303-15
Authors Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA
Title Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8457588
Journal Biochim Biophys Acta
Year 1993
Volume 1162
Pages 246-54
Authors Biely P, Kluepfel D, Morosoli R, Shareck F
Title Mode of action of three endo-beta-1,4-xylanases of Streptomyces lividans.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8471845
Journal Protein Expr Purif
Year 1993
Volume 4
Pages 120-9
Authors Grabski AC, Forrester IT, Patel R, Jeffries TW
Title Characterization and N-terminal amino acid sequences of beta-(1-4)endoxylanases from Streptomyces roseiscleroticus: purification incorporating a bioprocessing agent.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 7915112
Journal Biochem J
Year 1994
Volume 302
Pages 291-5
Authors Moreau A, Roberge M, Manin C, Shareck F, Kluepfel D, Morosoli R
Title Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 7765032
Journal Biosci Biotechnol Biochem
Year 1994
Volume 58
Pages 1041-4
Authors Yoshida S, Satoh T, Shimokawa S, Oku T, Ito T, Kusakabe I
Title Substrate specificity of Streptomyces beta-xylanase toward glucoxylan.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8000329
Journal Braz J Med Biol Res
Year 1994
Volume 27
Pages 1093-109
Authors Ferreira-Filho EX
Title The xylan-degrading enzyme system.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7764794
Journal Enzyme Microb Technol
Year 1994
Volume 16
Pages 420-4
Authors Moreau A, Shareck F, Kluepfel D, Morosoli R
Title Increase in catalytic activity and thermostability of the xylanase A of Streptomyces lividans 1326 by site-specific mutagenesis.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8306993
Journal Eur J Biochem
Year 1994
Volume 219
Pages 261-6
Authors Moreau A, Shareck F, Kluepfel D, Morosoli R
Title Alteration of the cleavage mode and of the transglycosylation reactions of the xylanase A of Streptomyces lividans 1326 by site-directed mutagenesis of the Asn173 residue.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8063693
Journal J Biol Chem
Year 1994
Volume 269
Pages 20811-4
Authors Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS
Title Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 7729513
Journal FEBS Lett
Year 1995
Volume 362
Pages 281-5
Authors Jenkins J, Lo Leggio L, Harris G, Pickersgill R
Title Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9201919
Journal Biochemistry
Year 1997
Volume 36
Pages 7769-75
Authors Roberge M, Shareck F, Morosoli R, Kluepfel D, Dupont C
Title Characterization of two important histidine residues in the active site of xylanase A from Streptomyces lividans, a family 10 glycanase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9118232
Journal Crit Rev Biotechnol
Year 1997
Volume 17
Pages 39-67
Authors Sunna A, Antranikian G
Title Xylanolytic enzymes from fungi and bacteria.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9006940
Journal J Biol Chem
Year 1997
Volume 272
Pages 2942-51
Authors Charnock SJ, Lakey JH, Virden R, Hughes N, Sinnott ML, Hazlewood GP, Pickersgill R, Gilbert HJ
Title Key residues in subsite F play a critical role in the activity of Pseudomonas fluorescens subspecies cellulosa xylanase A against xylooligosaccharides but not against highly polymeric substrates such as xylan.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9211898
Journal J Biol Chem
Year 1997
Volume 272
Pages 17523-30
Authors Spurway TD, Morland C, Cooper A, Sumner I, Hazlewood GP, O'Donnell AG, Pickersgill RW, Gilbert HJ
Title Calcium protects a mesophilic xylanase from proteinase inactivation and thermal unfolding.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9335171
Journal J Biotechnol
Year 1997
Volume 57
Pages 151-66
Authors Biely P, Vrsanska M, Tenkanen M, Kluepfel D
Title Endo-beta-1,4-xylanase families: differences in catalytic properties.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9194164
Journal Protein Eng
Year 1997
Volume 10
Pages 399-403
Authors Roberge M, Dupont C, Morosoli R, Shareck F, Kluepfel D
Title Asparagine-127 of xylanase A from Streptomyces lividans, a key residue in glycosyl hydrolases of superfamily 4/7: kinetic evidence for its involvement in stabilization of the catalytic intermediate.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 9681873
Journal Protein Eng
Year 1998
Volume 11
Pages 399-404
Authors Roberge M, Shareck F, Morosoli R, Kluepfel D, Dupont C
Title Site-directed mutagenesis study of a conserved residue in family 10 glycanases: histidine 86 of xylanase A from Streptomyces lividans.
Related PDB
Related UniProtKB
[21]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID
PubMed ID 10571062
Journal FEBS Lett
Year 1999
Volume 460
Pages 61-6
Authors Kaneko S, Kuno A, Fujimoto Z, Shimizu D, Machida S, Sato Y, Yura K, Go M, Mizuno H, Taira K, Kusakabe I, Hayashi K
Title An investigation of the nature and function of module 10 in a family F/10 xylanase FXYN of Streptomyces olivaceoviridis E-86 by module shuffling with the Cex of Cellulomonas fimi and by site-directed mutagenesis.
Related PDB 1xyf
Related UniProtKB Q7SI98
[22]
Resource
Comments
Medline ID
PubMed ID 10359093
Journal FEBS Lett
Year 1999
Volume 450
Pages 299-305
Authors Kuno A, Shimizu D, Kaneko S, Hasegawa T, Gama Y, Hayashi K, Kusakabe I, Taira K
Title Significant enhancement in the binding of p-nitrophenyl-beta-D-xylobioside by the E128H mutant F/10 xylanase from Streptomyces olivaceoviridis E-86.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 10570988
Journal Gene
Year 1999
Volume 238
Pages 93-101
Authors Sato Y, Niimura Y, Yura K, Go M
Title Module-intron correlation and intron sliding in family F/10 xylanase genes.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 10235626
Journal Protein Eng
Year 1999
Volume 12
Pages 251-7
Authors Roberge M, Shareck F, Morosoli R, Kluepfel D, Dupont C
Title Characterization of active-site aromatic residues in xylanase A from Streptomyces lividans.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 10884353
Journal J Mol Biol
Year 2000
Volume 300
Pages 575-85
Authors Fujimoto Z, Kuno A, Kaneko S, Yoshida S, Kobayashi H, Kusakabe I, Mizuno H
Title Crystal structure of Streptomyces olivaceoviridis E-86 beta-xylanase containing xylan-binding domain.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 10767281
Journal J Biol Chem
Year 2000
Volume 275
Pages 23027-33
Authors Andrews SR, Charnock SJ, Lakey JH, Davies GJ, Claeyssens M, Nerinckx W, Underwood M, Sinnott ML, Warren RA, Gilbert HJ
Title Substrate specificity in glycoside hydrolase family 10. Tyrosine 87 and leucine 314 play a pivotal role in discriminating between glucose and xylose binding in the proximal active site of Pseudomonas cellulosa xylanase 10A.
Related PDB 1e0v 1e0w 1e0x
Related UniProtKB
[27]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID
PubMed ID 11829503
Journal J Mol Biol
Year 2002
Volume 316
Pages 65-78
Authors Fujimoto Z, Kuno A, Kaneko S, Kobayashi H, Kusakabe I, Mizuno H
Title Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module.
Related PDB 1isv 1isw 1isx 1isy 1isz 1it0
Related UniProtKB Q7SI98
[28]
Resource
Comments
Medline ID
PubMed ID 11914070
Journal Biochemistry
Year 2002
Volume 41
Pages 4246-54
Authors Notenboom V, Boraston AB, Williams SJ, Kilburn DG, Rose DR
Title High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding.
Related PDB 1knl 1knm 1mc9
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 12744311
Journal Chem Commun (Camb)
Year 2003
Volume
Pages 944-5
Authors Gloster T, Williams SJ, Tarling CA, Roberts S, Dupont C, Jodoin P, Shareck F, Withers SG, Davies GJ
Title A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer.
Related PDB 1od8
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 15078885
Journal J Biol Chem
Year 2004
Volume 279
Pages 26619-26
Authors Kaneko S, Ichinose H, Fujimoto Z, Kuno A, Yura K, Go M, Mizuno H, Kusakabe I, Kobayashi H
Title Structure and function of a family 10 beta-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi Cex.
Related PDB
Related UniProtKB

Comments
This family belongs to the glycosidase family-10, which has a retaining mechanism (equatorial to equatorial conformation), and also a family of 4/7 superfamily, which has got catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold.
According to the literature [22], Glu236 and Glu128 (of 1ece) act as a nucleophile and acid-base, respectively. The catalysis proceeds through a dissociative-type (or SN1-like) mechanism, with a formation of oxocarbonium ion in the transition state, during the glycosylation of the active site.
During the glycosylation, Glu236 approaches the C1 atom of xylan substrate, whilst Glu128 protonates the leaving sugar group.
At the second stage, or during the deglycosylation, a water molecule can be activated by a general base, Glu128. This deglycosylation also goes through the dissociative-type reaction with an oxocarbonium ion in the transition state, in which water replaced the xylan leaving group in the first step.
According to the paper [19], the conserved residue at active site, Asn127, may stabilize the intermediate or transition state. Meanwhile, the paper [20] mentioned that His86 might modulate the acid-base catalyst (Glu128), by maintaining the elevated pKa of the catalytic residue.
Moreover, comparing the structural data with that of the other family-10 enzyme, xylanase (E.C. 3.2.1.8) (D00479 in EzCatDB), His207-Asp238 dyad seems to stabilize the leaving nucleophile, Glu236, during the deglycosylation.

Created Updated
2004-08-19 2009-02-26