3R44

Mycobacterium tuberculosis fatty acyl CoA synthetase

3R44 の概要

• エントリーDOI: 10.2210/pdb3r44/pdb
• 分子名称: fatty acyl CoA synthetase FADD13 (FATTY-ACYL-CoA SYNTHETASE), HISTIDINE, MALONATE ION, ... (4 entities in total)
• 機能のキーワード: acyl coa synthetase, ligase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56492.25

構造登録者

Andersson, C.S.,Martinez Molina, D.,Hogbom, M. (登録日: 2011-03-17, 公開日: 2012-02-08, 最終更新日: 2023-09-13)

主引用文献

Andersson, C.S.,Lundgren, C.A.,Magnusdottir, A.,Ge, C.,Wieslander, A.,Martinez Molina, D.,Hogbom, M.
The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme.
Structure, 20:1062-1070, 2012

PubMed Abstract: The Mycobacterium tuberculosis acid-induced operon MymA encodes the fatty acyl-CoA synthetase FadD13 and is essential for virulence and intracellular growth of the pathogen. Fatty acyl-CoA synthetases activate lipids before entering into the metabolic pathways and are also involved in transmembrane lipid transport. Unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length tested (C(26)). Here, we show that FadD13 is a peripheral membrane protein. The structure and mutational studies reveal an arginine- and aromatic-rich surface patch as the site for membrane interaction. The protein accommodates a hydrophobic tunnel that extends from the active site toward the positive patch and is sealed by an arginine-rich lid-loop at the protein surface. Based on this and previous data, we propose a structural basis for accommodation of lipid substrates longer than the enzyme and transmembrane lipid transport by vectorial CoA-esterification.

PubMed: 22560731
DOI: 10.1016/j.str.2012.03.012

実験手法

X-RAY DIFFRACTION (1.8 Å)