1DZT

RMLC FROM SALMONELLA TYPHIMURIUM

1DZT の概要

• エントリーDOI: 10.2210/pdb1dzt/pdb
• 関連するPDBエントリー: 1DZR
• 分子名称: DTDP-4-DEHYDRORHAMNOSE 3\,5-EPIMERASE, GLYCEROL, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: isomerase, 3\, 5 hexulose epimerase
• 由来する生物種: SALMONELLA TYPHIMURIUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42893.79

構造登録者

Naismith, J.H.,Giraud, M.F. (登録日: 2000-03-07, 公開日: 2000-04-18, 最終更新日: 2023-12-06)

主引用文献

Giraud, M.F.,Leonard, G.A.,Field, R.A.,Berlind, C.,Naismith, J.H.
Rmlc, the Third Enzyme of Dtdp-L-Rhamnose Pathway, is a New Class of Epimerase.
Nat.Struct.Biol., 7:398-, 2000

PubMed Abstract: Deoxythymidine diphosphate (dTDP)-L-rhamnose is the precursor of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. dTDP-L-rhamnose is synthesized from glucose-1-phosphate and deoxythymidine triphosphate (dTTP) via a pathway involving four distinct enzymes. This pathway does not exist in humans and the enzymes involved in dTDP-L-rhamnose synthesis are potential targets for the design of new therapeutic agents. Here, the crystal structure of dTDP-6-deoxy-D-xylo-4-hexulose 3,5 epimerase (RmlC, EC5.1.3.13) from Salmonella enterica serovar Typhimurium was determined. The third enzyme of the rhamnose biosynthetic pathway, RmlC epimerizes at two carbon centers, the 3 and 5 positions of the sugar ring. The structure was determined by multiwavelength anomalous diffraction to a resolution of 2.17 A. RmlC is a dimer and each monomer is formed mainly from two beta-sheets arranged in a beta-sandwich. The structure of a dTDP-phenol-RmlC complex shows the substrate-binding site to be located between the two beta-sheets; this site is formed from residues of both monomers. Sequence alignments of other RmlC enzymes confirm that this region is very highly conserved. The enzyme is distinct structurally from other epimerases known and thus, is the first example of a new class of carbohydrate epimerase.

PubMed: 10802738
DOI: 10.1038/75178

実験手法

X-RAY DIFFRACTION (2.2 Å)