1ogc

From Proteopedia

Revision as of 14:48, 5 November 2007

THE STRUCTURE OF BACILLUS SUBTILIS RBSD COMPLEXED WITH D-RIBOSE

Overview

RbsD is the only protein whose biochemical function is unknown among the, six gene products of the rbs operon involved in the active transport of, ribose. FucU, a paralogue of RbsD conserved from bacteria to human, is, also the only protein whose function is unknown among the seven gene, products of the l-fucose regulon. Here we report the crystal structures of, Bacillus subtilis RbsD, which reveals a novel decameric toroidal assembly, of the protein. Nuclear magnetic resonance and other studies on RbsD, reveal that the intersubunit cleft of the protein binds specific forms of, d-ribose, but it does not have an enzyme activity toward the sugar., Likewise, FucU binds l-fucose but lacks an enzyme activity toward this, sugar. We conclude that RbsD and FucU are cytoplasmic sugar-binding, proteins, a novel class of proteins whose functional role may lie in, helping influx of the sugar substrates.

About this Structure

1OGC is a Single protein structure of sequence from Bacillus subtilis with CL as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture., Kim MS, Shin J, Lee W, Lee HS, Oh BH, J Biol Chem. 2003 Jul 25;278(30):28173-80. Epub 2003 May 8. PMID:12738765

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