4V8W

Structure and conformational variability of the Mycobacterium tuberculosis fatty acid synthase multienzyme complex

これはPDB形式変換不可エントリーです。

4V8W の概要

• エントリーDOI: 10.2210/pdb4v8w/pdb
• 関連するPDBエントリー: 4BJD 4BJE
• EMDBエントリー: 2357
• 分子名称: TYPE-I FATTY ACID SYNTHASE, FLAVIN MONONUCLEOTIDE (2 entities in total)
• 機能のキーワード: hydrolase, fatty acid synthesis, sample heterogeneity, protein flexibility, codimensional principal component analysis
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 1982065.88

構造登録者

Ciccarelli, L.,Connell, S.R.,Enderle, M.,Mills, D.J.,Vonck, J.,Grininger, M. (登録日: 2013-04-18, 公開日: 2014-07-09, 最終更新日: 2024-05-08)

主引用文献

Ciccarelli, L.,Connell, S.R.,Enderle, M.,Mills, D.J.,Vonck, J.,Grininger, M.
Structure and Conformational Variability of the Mycobacterium Tuberculosis Fatty Acid Synthase Multienzyme Complex.
Structure, 21:1251-, 2013

PubMed Abstract: Antibiotic therapy in response to Mycobacterium tuberculosis infections targets de novo fatty acid biosynthesis, which is orchestrated by a 1.9 MDa type I fatty acid synthase (FAS). Here, we characterize M. tuberculosis FAS by single-particle cryo-electron microscopy and interpret the data by docking the molecular models of yeast and Mycobacterium smegmatis FAS. Our analysis reveals a porous barrel-like structure of considerable conformational variability that is illustrated by the identification of several conformational states with altered topology in the multienzymatic assembly. This demonstrates that the barrel-like structure of M. tuberculosis FAS is not just a static scaffold for the catalytic domains, but may play an active role in coordinating fatty acid synthesis. The conception of M. tuberculosis FAS as a highly dynamic assembly of domains revises the view on bacterial type I fatty acid synthesis and might inspire new strategies for inhibition of de novo fatty acid synthesis in M. tuberculosis.

PubMed: 23746808
DOI: 10.1016/J.STR.2013.04.023

実験手法

ELECTRON MICROSCOPY (17.5 Å)