1MWZ

Solution structure of the N-terminal domain of ZntA in the Zn(II)-form

1MWZ の概要

• エントリーDOI: 10.2210/pdb1mwz/pdb
• 関連するPDBエントリー: 1MWY
• NMR情報: BMRB: 5604
• 分子名称: ZntA, ZINC ION (2 entities in total)
• 機能のキーワード: open-faced beta-sandwich fold, beta-alpha-beta-beta-alpha-beta, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P37617
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8005.27

構造登録者

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Finney, L.A.,Outten, C.E.,O'Halloran, T.V. (登録日: 2002-10-01, 公開日: 2002-11-06, 最終更新日: 2024-05-22)

主引用文献

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Finney, L.A.,Outten, C.E.,O'Halloran, T.V.
A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the apo and Zn(II) forms of ZntA (46-118)
J.Mol.Biol., 323:883-897, 2002

PubMed Abstract: Zinc, a metal ion that functions in a wide variety of catalytic and structural sites in metalloproteins, is shown here to adopt a novel coordination environment in the Escherichia coli transport protein ZntA. The ZntA protein is a P-type ATPase that pumps zinc out of the cytoplasm and into the periplasm. It is physiologically selective for Zn(II) and functions with metalloregulatory proteins in the cell to keep the zinc quota within strict limits. Yet, the N-terminal cytoplasmic domain contains a region that is highly homologous to the yeast Cu(I) metallochaperone Atx1. To investigate how the structure of this region may influence its function, this fragment, containing residues 46-118, has been cloned out of the gene and overexpressed. We report here the solution structure of this fragment as determined by NMR. Both the apo and Zn(II)-ZntA(46-118) structures have been determined. It contains a previously unknown protein coordination site for zinc that includes two cysteine residues, Cys59 and Cys62, and a carboxylate residue, Asp58. The solvent accessibility of this site is also remarkably high, a feature that increasingly appears to be a characteristic of domains of heavy metal ion transport proteins. The participation of Asp58 in this ZntA metal ion binding site may play an important role in modulating the relative affinities and metal exchange rates for Zn(II)/Pb(II)/Cd(II) as compared with other P-type ATPases, which are selective for Cu(I) or Ag(I).

PubMed: 12417201
DOI: 10.1016/S0022-2836(02)01007-0

実験手法

SOLUTION NMR