1oge

The Structure of Bacillus subtilis RbsD complexed with Ribose 5-phosphate

spinqualitylabelsall models 1oge, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1oge is a 5 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: CL, RP5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RBSD_BACSU Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose (By similarity).[HAMAP-Rule:MF_01661] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribose-binding protein

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