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pubmed-article:12738765pubmed:abstractTextRbsD 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.lld:pubmed
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pubmed-article:12738765pubmed:authorpubmed-author:LeeWeontaeWlld:pubmed
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pubmed-article:12738765pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:12738765pubmed:articleTitleCrystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture.lld:pubmed
pubmed-article:12738765pubmed:affiliationCenter for Biomolecular Recognition and Division of Molecular and Life Science, Department of Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Korea.lld:pubmed
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