5MLK

Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)

5MLK の概要

• エントリーDOI: 10.2210/pdb5mlk/pdb
• 分子名称: Acetyl-COA carboxylase (2 entities in total)
• 機能のキーワード: biotin dependant carboxylase, grasp, ligase
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130925.30

構造登録者

Bennett, M.D.,Hogbom, M. (登録日: 2016-12-07, 公開日: 2017-03-08, 最終更新日: 2024-05-08)

主引用文献

Bennett, M.,Hogbom, M.
Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis.
FEBS Open Bio, 7:620-626, 2017

PubMed Abstract: Biotin-dependent acetyl-CoA carboxylases catalyze the committed step in type II fatty acid biosynthesis, the main route for production of membrane phospholipids in bacteria, and are considered a key target for antibacterial drug discovery. Here we describe the first structure of AccA3, an essential component of the acetyl-CoA carboxylase system in (MTb). The structure, sequence comparisons, and modeling of ligand-bound states reveal that the ATP cosubstrate-binding site shows distinct differences compared to other bacterial and eukaryotic biotin carboxylases, including all human homologs. This suggests the possibility to design MTb AccA3 subtype-specific inhibitors.

PubMed: 28469974
DOI: 10.1002/2211-5463.12212

実験手法

X-RAY DIFFRACTION (1.939 Å)