1NZC

The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose

1NZC の概要

• エントリーDOI: 10.2210/pdb1nzc/pdb
• 関連するPDBエントリー: 1NXM 1NYW
• 分子名称: dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase, THYMIDINE-5'-DIPHOSPHO-BETA-D-XYLOSE, NICKEL (II) ION, ... (4 entities in total)
• 機能のキーワード: jelly roll-like structure; beta sheet, isomerase
• 由来する生物種: Streptococcus suis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 92207.78

構造登録者

Dong, C.,Major, L.L.,Allen, A.,Blankenfeldt, W.,Maskell, D.,Naismith, J.H. (登録日: 2003-02-17, 公開日: 2003-06-24, 最終更新日: 2023-08-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)