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1exp

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[[Image:1exp.gif|left|200px]]
[[Image:1exp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1exp |SIZE=350|CAPTION= <scene name='initialview01'>1exp</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1exp", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ABC:Acid+Base+Catalyst'>ABC</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile,+Covalently+Linked+To+The+Fluoroce+...'>NUC</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=G2F:2-DEOXY-2FLUORO-GLUCOSE'>G2F</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>
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|ACTIVITY=
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|GENE=
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{{STRUCTURE_1exp| PDB=1exp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1exp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exp OCA], [http://www.ebi.ac.uk/pdbsum/1exp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1exp RCSB]</span>
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'''BETA-1,4-GLYCANASE CEX-CD'''
'''BETA-1,4-GLYCANASE CEX-CD'''
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[[Category: White, A.]]
[[Category: White, A.]]
[[Category: Withers, S G.]]
[[Category: Withers, S G.]]
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[[Category: cellulose degradation]]
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[[Category: Cellulose degradation]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: repeat]]
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[[Category: Repeat]]
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[[Category: signal]]
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[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:38:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:41 2008''
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Revision as of 12:38, 2 May 2008

Image:1exp.gif

Template:STRUCTURE 1exp

BETA-1,4-GLYCANASE CEX-CD


Overview

The three-dimensional structure of a catalytically competent glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two invariant carboxylates, Glu 233, as supported in solution by 19F-NMR studies. The resulting ester linkage is coplanar with the cyclic oxygen of the proximal saccharide and is inferred to form a strong hydrogen bond with the 2-hydroxyl of that saccharide unit in natural substrates. The active-site architecture of this covalent intermediate gives insights into both the classical double-displacement catalytic mechanism and the basis for the enzyme's specificity.

About this Structure

1EXP is a Single protein structure of sequence from Cellulomonas fimi. Full crystallographic information is available from OCA.

Reference

Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase., White A, Tull D, Johns K, Withers SG, Rose DR, Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541 Page seeded by OCA on Fri May 2 15:38:39 2008

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