PMID:12738765
| Citation |
Kim, MS, Shin, J, Lee, W, Lee, HS and Oh, BH (2003) Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. J. Biol. Chem. 278:28173-80 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1074/jbc.M304523200 |
| Keywords |
Amino Acid Sequence; Bacillus subtilis/metabolism; Binding Sites; Calorimetry; Crystallography, X-Ray; Cytoplasm/metabolism; Escherichia coli/metabolism; Fucose/metabolism; Glycerol/chemistry; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins/chemistry; Monosaccharide Transport Proteins/metabolism; Polymerase Chain Reaction; Protein Binding; Protein Folding; Protein Structure, Secondary; Ribose/chemistry; Sequence Homology, Amino Acid |
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