Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture
SCIE
SCOPUS
- Title
- Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture
- Authors
- Kim, MS; Shin, J; Lee, WT; Lee, HS; Oh, BH
- Date Issued
- 2003-07-25
- Publisher
- American Society for biochemistry and molecular biology
- 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/40825
- DOI
- 10.1074/jbc.M304523200
- ISSN
- 0021-9258
- Article Type
- Article
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 278, no. 30, page. 28173 - 28180, 2003-07-25
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.