1EP0

HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

1EP0 の概要

• エントリーDOI: 10.2210/pdb1ep0/pdb
• 関連するPDBエントリー: 1EPZ
• 分子名称: DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE (2 entities in total)
• 機能のキーワード: racemase, dtdp-4-dehydrorhamnose epimerase, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, isomerase
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21702.33

構造登録者

Christendat, D.,Saridakis, V.,Bochkarev, A.,Pai, E.F.,Arrowsmith, C.H.,Edwards, A.M.,Northeast Structural Genomics Consortium (NESG) (登録日: 2000-03-24, 公開日: 2000-12-13, 最終更新日: 2024-02-07)

主引用文献

Christendat, D.,Saridakis, V.,Dharamsi, A.,Bochkarev, A.,Pai, E.F.,Arrowsmith, C.H.,Edwards, A.M.
Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP.
J.Biol.Chem., 275:24608-24612, 2000

PubMed Abstract: Deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-d-hexulose 3, 5-epimerase (RmlC) is involved in the biosynthesis of dTDP-l-rhamnose, which is an essential component of the bacterial cell wall. The crystal structure of RmlC from Methanobacterium thermoautotrophicum was determined in the presence and absence of dTDP, a substrate analogue. RmlC is a homodimer comprising a central jelly roll motif, which extends in two directions into longer beta-sheets. Binding of dTDP is stabilized by ionic interactions to the phosphate group and by a combination of ionic and hydrophobic interactions with the base. The active site, which is located in the center of the jelly roll, is formed by residues that are conserved in all known RmlC sequence homologues. The conservation of the active site residues suggests that the mechanism of action is also conserved and that the RmlC structure may be useful in guiding the design of antibacterial drugs.

PubMed: 10827167
DOI: 10.1074/jbc.C000238200

実験手法

X-RAY DIFFRACTION (1.5 Å)