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PDBsum entry 2pc8
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References listed in PDB file
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Key reference
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Title
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Carbohydrate binding sites in candida albicans exo-β-1,3-Glucanase and the role of the phe-Phe 'Clamp' At the active site entrance.
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Authors
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W.M.Patrick,
Y.Nakatani,
S.M.Cutfield,
M.L.Sharpe,
R.J.Ramsay,
J.F.Cutfield.
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Ref.
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Febs J, 2010,
277,
4549-4561.
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PubMed id
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Abstract
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No abstract given.
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Secondary reference #1
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Title
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The structure of the exo-Beta-(1,3)-Glucanase from candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases.
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Authors
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S.M.Cutfield,
G.J.Davies,
G.Murshudov,
B.F.Anderson,
P.C.Moody,
P.A.Sullivan,
J.F.Cutfield.
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Ref.
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J Mol Biol, 1999,
294,
771-783.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. Enzyme glycosylation mechanism and two inhibitors of exo-b-(1,3)-glucanase. (a) Formation of the
covalent glycosyl-enzyme intermediate is presumed to proceed through an oxo-carbenium ion-like transition state
and involve nucleophile Glu292 and proton donor Glu192, which act on the glycosidic bond at the non-reducing end
of a b-1,3-glucan chain. The chemical structures of the glucosidase inhibitor, castanospermine, and of the mechanism-
based inactivator 2 ,4 -dinitrophenyl-2-deoxy-2-fluoro-b-D-glucopyranoside are labelled (b) and (c) respectively.
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Figure 6.
Figure 6. GRASP electrostatic surface representation of the binding site of Exg with the two bound saccharides,
following reaction of Exg crystals with the mechanism-based inhibitor DNP-DFG (see Figure 1(c)). Covalently bound
DFG (green spheres) is at the bottom of the pocket (shown left) while a second DFG (yellow spheres) is held between
two phenylalanyl side-chains at the pocket entrance (shown right).
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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