1exp: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1exp|  PDB=1exp  |  SCENE=  }}  
{{STRUCTURE_1exp|  PDB=1exp  |  SCENE=  }}  


'''BETA-1,4-GLYCANASE CEX-CD'''
===BETA-1,4-GLYCANASE CEX-CD===




==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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{{ABSTRACT_PUBMED_8564541}}


==About this Structure==
==About this Structure==
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[[Category: Repeat]]
[[Category: Repeat]]
[[Category: Signal]]
[[Category: Signal]]
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