Novel stereospecificity of the l-arabinose-binding protein

ABSTRACT Tertiary structure refinement at 1.7 Å resolution of the liganded form of L-arabinose-binding protein from _Escherichia coli_ has revealed a novel binding site geometry which

accommodates both α- and β-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 Access through your institution Buy or subscribe

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INFORMATION AUTHORS AND AFFILIATIONS * Department of Biochemistry, Rice University, Houston, Texas, 77251, USA Florante A. Quiocho & Nand K. Vyas Authors * Florante A. Quiocho View

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PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Quiocho, F., Vyas, N. Novel stereospecificity of the L-arabinose-binding protein. _Nature_ 310, 381–386 (1984).

https://doi.org/10.1038/310381a0 Download citation * Received: 09 January 1984 * Accepted: 11 May 1984 * Issue Date: 02 August 1984 * DOI: https://doi.org/10.1038/310381a0 SHARE THIS ARTICLE

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