1abe | pdb_00001abe

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Revision as of 08:37, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1abe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1abe, resolution 1.7Å" /> '''NOVEL STEREOSPECIFICI...)
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File:1abe.jpg


1abe, resolution 1.7Å

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NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

Overview

Tertiary structure refinement at 1.7 A resolution of the liganded form of, L-arabinose-binding protein from Escherichia coli has revealed a novel, binding site geometry which accommodates both alpha- and beta-anomers of, L-arabinose. This detailed structure analysis provides new understanding, of protein-sugar interaction, the process by which the binding protein, minimizes the difference in the stability of the two bound sugar anomers, and the roles of periplasmic binding proteins in active transport.

About this Structure

1ABE is a Single protein structure of sequence from Escherichia coli. This structure superseeds the now removed PDB entry 1ABP. Full crystallographic information is available from OCA.

Reference

Novel stereospecificity of the L-arabinose-binding protein., Quiocho FA, Vyas NK, Nature. 1984 Aug 2-8;310(5976):381-6. PMID:6379466

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