6O6N

Structure of the regulator FasR from Mycobacterium tuberculosis in complex with C20-CoA

6O6N の概要

• エントリーDOI: 10.2210/pdb6o6n/pdb
• 分子名称: TetR family transcriptional regulator, Arachinoyl-CoA, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: tetr-like transcription factor, fatty acid biosynthesis regulation, transcription
• 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: 22725.32

構造登録者

Larrieux, N.,Trajtenberg, F.,Lara, J.,Gramajo, H.,Buschiazzo, A. (登録日: 2019-03-07, 公開日: 2020-03-11, 最終更新日: 2024-03-13)

主引用文献

Lara, J.,Diacovich, L.,Trajtenberg, F.,Larrieux, N.,Malchiodi, E.L.,Fernandez, M.M.,Gago, G.,Gramajo, H.,Buschiazzo, A.
Mycobacterium tuberculosis FasR senses long fatty acyl-CoA through a tunnel and a hydrophobic transmission spine.
Nat Commun, 11:3703-3703, 2020

PubMed Abstract: Mycobacterium tuberculosis is a pathogen with a unique cell envelope including very long fatty acids, implicated in bacterial resistance and host immune modulation. FasR is a TetR-like transcriptional activator that plays a central role in sensing mycobacterial long-chain fatty acids and regulating lipid biosynthesis. Here we disclose crystal structures of M. tuberculosis FasR in complex with acyl effector ligands and with DNA, uncovering its molecular sensory and switching mechanisms. A long tunnel traverses the entire effector-binding domain, enabling long fatty acyl effectors to bind. Only when the tunnel is entirely occupied, the protein dimer adopts a rigid configuration with its DNA-binding domains in an open state, leading to DNA dissociation. The protein-folding hydrophobic core connects the two domains, and is completed into a continuous spine when the effector binds. Such a transmission spine is conserved in a large number of TetR-like regulators, offering insight into effector-triggered allosteric functional control.

PubMed: 32710080
DOI: 10.1038/s41467-020-17504-x

実験手法

X-RAY DIFFRACTION (1.7 Å)