1nzc
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Revision as of 21:58, 24 November 2007
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The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose
Overview
Nature achieves the epimerization of carbohydrates by a variety of, chemical routes. One common route is that performed by the class of enzyme, defined by dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC) from the, rhamnose pathway. Earlier studies failed to identify the key residues in, catalysis. We report the 1.3 A structure of RmlC from Streptococcus suis, type 2 and its complexes with dTDP-D-glucose and dTDP-D-xylose. The, streptococcal RmlC enzymes belong to a separate subgroup, sharing only 25%, identity with RmlC from other bacteria, yet the S. suis enzyme has similar, kinetic properties and structure to other RmlC enzymes. Structure, sequence alignment, and mutational analysis have now allowed reliable, identification of the catalytic residues and their roles.
About this Structure
1NZC is a Single protein structure of sequence from Streptococcus suis with NI and TDX as ligands. Active as dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13 Full crystallographic information is available from OCA.
Reference
High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme., Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH, Structure. 2003 Jun;11(6):715-23. PMID:12791259
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