- PDB-7nh9: structure of the full-length CmaX protein -
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基本情報
登録情報
データベース: PDB / ID: 7nh9
タイトル
structure of the full-length CmaX protein
要素
CmaX protein
キーワード
TRANSPORT PROTEIN / divalent transport / zinc transporter / CorA family / membrane protein
機能・相同性
Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB / CorA-like Mg2+ transporter protein / cobalt ion transmembrane transporter activity / magnesium ion transmembrane transporter activity / cobalt ion binding / plasma membrane => GO:0005886 / magnesium ion binding / CmaX protein
Netherlands Organisation for Scientific Research (NWO)
740.018.011
引用
ジャーナル: Int J Biol Macromol / 年: 2021 タイトル: Structural and biochemical characterization of a novel ZntB (CmaX) transporter protein from Pseudomonas aeruginosa. 著者: Artem Stetsenko / Pavlo Stehantsev / Natalia O Dranenko / Mikhail S Gelfand / Albert Guskov / 要旨: 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, ...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.