High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme

Dong, Changjiang, Major, Louise L., Allen, Andrew, Blankenfeldt, Wulf, Maskell, Duncan and Naismith, James H. (2003) High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme. Structure, 11 (6). pp. 715-723. ISSN 0969-2126

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Abstract

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.

Item Type:	Article
Uncontrolled Keywords:	bacterial proteins,binding sites,carbohydrate epimerases,crystallography x-ray,ligands,molecular models,protein binding,tertiary protein structure,streptococcus suis
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups:	Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology
Depositing User:	Pure Connector
Date Deposited:	17 Nov 2014 12:56
Last Modified:	08 Mar 2024 00:50
URI:	https://ueaeprints.uea.ac.uk/id/eprint/50995
DOI:	10.1016/S0969-2126(03)00098-4

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