6CTD

C-terminal domain truncation of the Mycobacterium tuberculosis Mechanosensitive Channel of Large Conductance MscL

6CTD の概要

• エントリーDOI: 10.2210/pdb6ctd/pdb
• 分子名称: Large-conductance mechanosensitive channel, GOLD ION (2 entities in total)
• 機能のキーワード: channel mechanosensitive mycobacterium tuberculosis, membrane protein
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 131908.14

構造登録者

Herrera, N.,Rees, D.C. (登録日: 2018-03-22, 公開日: 2018-10-10, 最終更新日: 2024-03-13)

主引用文献

Herrera, N.,Maksaev, G.,Haswell, E.S.,Rees, D.C.
Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance.
Sci Rep, 8:14566-14566, 2018

PubMed Abstract: Microbial survival in dynamic environments requires the ability to successfully respond to abrupt changes in osmolarity. The mechanosensitive channel of large conductance (MscL) is a ubiquitous channel that facilitates the survival of bacteria and archaea under severe osmotic downshock conditions by relieving excess turgor pressure in response to increased membrane tension. A prominent structural feature of MscL, the cytoplasmic C-terminal domain, has been suggested to influence channel assembly and function. In this report, we describe the X-ray crystal structure and electrophysiological properties of a C-terminal domain truncation of the Mycobacterium tuberculosis MscL (MtMscLΔC). A crystal structure of MtMscLΔC solubilized in the detergent n-dodecyl-β-D-maltopyranoside reveals the pentameric, closed state-like architecture for the membrane spanning region observed in the previously solved full-length MtMscL. Electrophysiological characterization demonstrates that MtMscLΔC retains mechanosensitivity, but with conductance and tension sensitivity more closely resembling full length EcMscL than MtMscL. This study establishes that the C-terminal domain of MtMscL is not required for oligomerization of the full-length channel, but rather influences the tension sensitivity and conductance properties of the channel. The collective picture that emerges from these data is that each MscL channel structure has characteristic features, highlighting the importance of studying multiple homologs.

PubMed: 30275500
DOI: 10.1038/s41598-018-32536-6

実験手法

X-RAY DIFFRACTION (5.8 Å)