| First Author | Kim MS | Year | 2003 |
| Journal | J Biol Chem | Volume | 278 |
| Issue | 30 | Pages | 28173-80 |
| PubMed ID | 12738765 | Mgi Jnum | J:84532 |
| Mgi Id | MGI:2668259 | Doi | 10.1074/jbc.M304523200 |
| Citation | Kim MS, et al. (2003) Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. J Biol Chem 278(30):28173-80 |
| abstractText | 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. |
