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1abe

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{{STRUCTURE_1abe| PDB=1abe | SCENE= }}
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'''NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN'''
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===NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 6379466 is the PubMed ID number.
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{{ABSTRACT_PUBMED_6379466}}
==About this Structure==
==About this Structure==
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[[Category: Vyas, N K.]]
[[Category: Vyas, N K.]]
[[Category: Binding protein]]
[[Category: Binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:04:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:31:58 2008''

Revision as of 13:32, 30 June 2008

Image:1abe.png

Template:STRUCTURE 1abe

NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

Template:ABSTRACT PUBMED 6379466

About this Structure

1ABE is a Single protein structure of sequence from Escherichia coli. This structure supersedes 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

Page seeded by OCA on Mon Jun 30 16:31:58 2008

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