7NH9

structure of the full-length CmaX protein

7NH9 の概要

• エントリーDOI: 10.2210/pdb7nh9/pdb
• EMDBエントリー: 12321
• 分子名称: CmaX protein (1 entity in total)
• 機能のキーワード: divalent transport, zinc transporter, cora family, membrane protein, transport protein
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 206825.10

構造登録者

Stetsenko, A.,Stehantsev, P.,Guskov, A. (登録日: 2021-02-10, 公開日: 2021-07-07, 最終更新日: 2025-07-09)

主引用文献

Stetsenko, A.,Stehantsev, P.,Dranenko, N.O.,Gelfand, M.S.,Guskov, A.
Structural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa.
Int.J.Biol.Macromol., 184:760-767, 2021

PubMed Abstract: The 2-TM-GxN family of membrane proteins is widespread in prokaryotes and plays an important role in transport of divalent cations. The canonical signature motif, which is also a selectivity filter, has a composition of Gly-Met-Asn. Some members though deviate from this composition, however no data are available as to whether this has any functional implications. Here we report the functional and structural analysis of CmaX protein from a pathogenic Pseudomonas aeruginosa bacterium, which has a Gly-Ile-Asn signature motif. CmaX readily transports Zn, Mg, Cd, Ni and Co ions, but it does not utilize proton-symport as does ZntB from Escherichia coli. Together with the bioinformatics analysis, our data suggest that deviations from the canonical signature motif do not reveal any changes in substrate selectivity or transport and easily alter in course of evolution.

PubMed: 34175341
DOI: 10.1016/j.ijbiomac.2021.06.130

実験手法

ELECTRON MICROSCOPY (3.03 Å)