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1exp

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{{STRUCTURE_1exp| PDB=1exp | SCENE= }}
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'''BETA-1,4-GLYCANASE CEX-CD'''
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===BETA-1,4-GLYCANASE CEX-CD===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8564541 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8564541}}
==About this Structure==
==About this Structure==
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Revision as of 23:10, 30 June 2008

Image:1exp.png

Template:STRUCTURE 1exp

BETA-1,4-GLYCANASE CEX-CD

Template:ABSTRACT PUBMED 8564541

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 Tue Jul 1 02:10:43 2008

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