1OGC

The Structure of Bacillus subtilis RbsD complexed with D-ribose

Summary for 1OGC

• Entry DOI: 10.2210/pdb1ogc/pdb
• Related: 1OGD 1OGE 1OGF
• Descriptor: HIGH AFFINITY RIBOSE TRANSPORT PROTEIN RBSD, CHLORIDE ION (3 entities in total)
• Functional Keywords: ribose, transport, sugar transport
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 5
• Total formula weight: 71293.10

Authors

Kim, M.-S.,Oh, B.-H. (deposition date: 2003-04-30, release date: 2003-09-01, Last modification date: 2024-05-08)

Primary citation

Kim, M.-S.,Shin, J.,Lee, W.,Lee, H.-S.,Oh, B.-H.
Crystal Structures of Rbsd Leading to the Identification of Cytoplasmic Sugar-Binding Proteins with a Novel Folding Architecture
J.Biol.Chem., 278:28173-, 2003

PubMed Abstract: 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.

PubMed: 12738765
DOI: 10.1074/JBC.M304523200

Experimental method

X-RAY DIFFRACTION (2 Å)