6IDS

Crystal structure of Vibrio cholerae MATE transporter VcmN D35N mutant

6IDS の概要

• エントリーDOI: 10.2210/pdb6ids/pdb
• 分子名称: MATE family efflux transporter, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total)
• 機能のキーワード: mate multidrug transporter, transport protein
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48592.17

構造登録者

Kusakizako, T.,Claxton, D.P.,Tanaka, Y.,Maturana, A.D.,Kuroda, T.,Ishitani, R.,Mchaourab, H.S.,Nureki, O. (登録日: 2018-09-11, 公開日: 2019-01-16, 最終更新日: 2024-03-27)

主引用文献

Kusakizako, T.,Claxton, D.P.,Tanaka, Y.,Maturana, A.D.,Kuroda, T.,Ishitani, R.,Mchaourab, H.S.,Nureki, O.
Structural Basis of H+-Dependent Conformational Change in a Bacterial MATE Transporter.
Structure, 27:293-, 2019

PubMed Abstract: Multidrug and toxic compound extrusion (MATE) transporters efflux toxic compounds using a Na or H gradient across the membrane. Although the structures of MATE transporters have been reported, the cation-coupled substrate transport mechanism remains controversial. Here we report crystal structures of VcmN, a Vibrio cholerae MATE transporter driven by the H gradient. High-resolution structures in two distinct conformations associated with different pHs revealed that the rearrangement of the hydrogen-bonding network around the conserved Asp35 induces the bending of transmembrane helix 1, as in the case of the H-coupled Pyrococcus furiosus MATE transporter. We also determined the crystal structure of the D35N mutant, which captured a unique conformation of TM1 facilitated by an altered hydrogen-bonding network. Based on the present results, we propose a common step in the transport cycle shared among prokaryotic H-coupled MATE transporters.

PubMed: 30449688
DOI: 10.1016/j.str.2018.10.004

実験手法

X-RAY DIFFRACTION (2.79 Å)