1ogd | pdb_00001ogd
THE STRUCTURE OF BACILLUS SUBTILIS RBSD COMPLEXED WITH D-RIBOSE
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| 1ogd, resolution 1.95Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CL, RIP | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
1OGD is a Single protein structure of sequence from Bacillus subtilis. 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
Page seeded by OCA on Sun Mar 30 22:44:57 2008
