1abe | pdb_00001abe
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| 1abe, resolution 1.7Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 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
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