Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture

Min Sung Kim, Joon Shin, Weontae Lee, Heung Soo Lee, Byung Ha Oh

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18 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)28173-28180
Number of pages8
JournalJournal of Biological Chemistry
Volume278
Issue number30
DOIs
Publication statusPublished - 2003 Jul 25

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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