2QJ3

Mycobacterium tuberculosis FabD

2QJ3 の概要

• エントリーDOI: 10.2210/pdb2qj3/pdb
• 分子名称: Malonyl CoA-acyl carrier protein transacylase, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: malonyl-coa, fatty acid synthase, mycolic acids, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66266.36

構造登録者

Ghadbane, H.,Brown, A.K.,Kremer, L.,Besra, G.S.,Futterer, K. (登録日: 2007-07-06, 公開日: 2007-09-04, 最終更新日: 2024-10-09)

主引用文献

Ghadbane, H.,Brown, A.K.,Kremer, L.,Besra, G.S.,Futterer, K.
Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT).
Acta Crystallogr.,Sect.F, 63:831-835, 2007

PubMed Abstract: Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.

PubMed: 17909282
DOI: 10.1107/S1744309107042455

実験手法

X-RAY DIFFRACTION (3 Å)