1xic: Difference between revisions

Revision as of 15:34, 28 July 2008

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File:1xic.png

Template:STRUCTURE 1xic

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASEMODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

Template:ABSTRACT PUBMED 15299449

About this StructureAbout this Structure

1XIC is a Single protein structure of sequence from Streptomyces rubiginosus. Full crystallographic information is available from OCA.

ReferenceReference

Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:15299449

Page seeded by OCA on Mon Jul 28 15:34:38 2008

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-'''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''
+===MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE===
-==Overview==
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-Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that there are a variety of binding modes. These vary in the manner in which the substrate or its analogue extend, on binding, across the carboxy end of the (betaalpha)(8)-barrel structure. These binding sites are His54 and the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated.
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 [[Category: Carrell, H L.]]
 [[Category: Glusker, J P.]]
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