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PDBsum entry 2ww3
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Structure of the family gh92 inverting mannosidase bt3990 from bacteroides thetaiotaomicron vpi-5482 in complex with thiomannobioside
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Structure:
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Putative alpha-1,2-mannosidase. Chain: a, b, c, d, e, f. Fragment: residues 20-755. Synonym: mannosidase. Engineered: yes
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Source:
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Bacteroides thetaiotaomicron. Organism_taxid: 226186. Strain: vpi-5482. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.10Å
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R-factor:
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0.193
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R-free:
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0.244
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Authors:
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M.D.L.Suits,Y.Zhu,A.J.Thompson,H.J.Gilbert,G.J.Davies
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Key ref:
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Y.Zhu
et al.
(2010).
Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.
Nat Chem Biol,
6,
125-132.
PubMed id:
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Date:
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21-Oct-09
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Release date:
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26-Jan-10
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PROCHECK
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Headers
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References
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Q8A0N1
(Q8A0N1_BACTN) -
Alpha-1,2-mannosidase from Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
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Seq:
Struc:
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755 a.a.
736 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Nat Chem Biol
6:125-132
(2010)
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PubMed id:
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Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.
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Y.Zhu,
M.D.Suits,
A.J.Thompson,
S.Chavan,
Z.Dinev,
C.Dumon,
N.Smith,
K.W.Moremen,
Y.Xiang,
A.Siriwardena,
S.J.Williams,
H.J.Gilbert,
G.J.Davies.
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ABSTRACT
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Colonic bacteria, exemplified by Bacteroides thetaiotaomicron, play a key role
in maintaining human health by harnessing large families of glycoside hydrolases
(GHs) to exploit dietary polysaccharides and host glycans as nutrients. Such GH
family expansion is exemplified by the 23 family GH92 glycosidases encoded by
the B. thetaiotaomicron genome. Here we show that these are alpha-mannosidases
that act via a single displacement mechanism to utilize host N-glycans. The
three-dimensional structure of two GH92 mannosidases defines a family of
two-domain proteins in which the catalytic center is located at the domain
interface, providing acid (glutamate) and base (aspartate) assistance to
hydrolysis in a Ca(2+)-dependent manner. The three-dimensional structures of the
GH92s in complex with inhibitors provide insight into the specificity, mechanism
and conformational itinerary of catalysis. Ca(2+) plays a key catalytic role in
helping distort the mannoside away from its ground-state (4)C(1) chair
conformation toward the transition state.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.L.Cheung,
G.Wilcox,
K.Z.Walker,
N.P.Shah,
B.Strauss,
J.F.Ashton,
and
L.Stojanovska
(2011).
Fermentation of calcium-fortified soya milk does not appear to enhance acute calcium absorption in osteopenic post-menopausal women.
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Br J Nutr,
105,
282-286.
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M.D.Suits,
Y.Zhu,
E.J.Taylor,
J.Walton,
D.L.Zechel,
H.J.Gilbert,
and
G.J.Davies
(2010).
Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidase.
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PLoS One,
5,
e9006.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
