1NYW

The high resolution structures of RmlC from Streptoccus suis in complex with dTDP-D-glucose

Summary for 1NYW

• Entry DOI: 10.2210/pdb1nyw/pdb
• Related: 1NXM 1NZC
• Descriptor: dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase, 2'DEOXY-THYMIDINE-5'-DIPHOSPHO-ALPHA-D-GLUCOSE (3 entities in total)
• Functional Keywords: jelly roll-like structure; beta sheet, isomerase
• Biological source: Streptococcus suis
• Total number of polymer chains: 2
• Total formula weight: 46105.25

Authors

Dong, C.,Major, L.L.,Allen, A.,Blankenfeldt, W.,Maskell, D.,Naismith, J.H. (deposition date: 2003-02-14, release date: 2003-06-24, Last modification date: 2024-02-14)

Primary citation

Dong, C.,Major, L.L.,Allen, A.,Blankenfeldt, W.,Maskell, D.,Naismith, J.H.
High-Resolution Structures of RmlC from Streptococcus suis in Complex with Substrate Analogs Locate the Active Site of This Class of Enzyme
Structure, 11:715-723, 2003

PubMed 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.

PubMed: 12791259
DOI: 10.1016/S0969-2126(03)00098-4

Experimental method

X-RAY DIFFRACTION (1.6 Å)