1ogf
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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, . | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OGF is a | + | 1OGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CL and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:03:52 2007'' |
Revision as of 12:58, 5 November 2007
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THE STRUCTURE OF BACILLUS SUBTILIS RBSD COMPLEXED WITH GLYCEROL
Overview
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.
About this Structure
1OGF is a Single protein structure of sequence from Bacillus subtilis with CL and GOL as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture., Kim MS, Shin J, Lee W, Lee HS, Oh BH, J Biol Chem. 2003 Jul 25;278(30):28173-80. Epub 2003 May 8. PMID:12738765
Page seeded by OCA on Mon Nov 5 15:03:52 2007
Categories: Bacillus subtilis | Single protein | Kim, M.S. | Oh, B.H. | CL | GOL | Ribose | Sugar transport | Transport
