1mwz

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

Structural highlights

1mwz is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZNTA_ECOLI Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661).^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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).

A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118).,Banci L, Bertini I, Ciofi-Baffoni S, Finney LA, Outten CE, O'Halloran TV J Mol Biol. 2002 Nov 8;323(5):883-97. PMID:12417201^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sharma R, Rensing C, Rosen BP, Mitra B. The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli. J Biol Chem. 2000 Feb 11;275(6):3873-8. PMID:10660539 doi:10.1074/jbc.275.6.3873
↑ Dutta SJ, Liu J, Stemmler AJ, Mitra B. Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: effect on metal selectivity and activity. Biochemistry. 2007 Mar 27;46(12):3692-703. PMID:17326661 doi:10.1021/bi0616394
↑ Beard SJ, Hashim R, Membrillo-Hernández J, Hughes MN, Poole RK. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol Microbiol. 1997 Sep;25(5):883-91. PMID:9364914 doi:10.1111/j.1365-2958.1997.mmi518.x
↑ Rensing C, Mitra B, Rosen BP. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14326-31. PMID:9405611 doi:10.1073/pnas.94.26.14326
↑ Rensing C, Sun Y, Mitra B, Rosen BP. Pb(II)-translocating P-type ATPases. J Biol Chem. 1998 Dec 4;273(49):32614-7. PMID:9830000 doi:10.1074/jbc.273.49.32614
↑ Banci L, Bertini I, Ciofi-Baffoni S, Finney LA, Outten CE, O'Halloran TV. 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. 2002 Nov 8;323(5):883-97. PMID:12417201

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OCA

[1] Sharma R, Rensing C, Rosen BP, Mitra B. The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli. J Biol Chem. 2000 Feb 11;275(6):3873-8. PMID:10660539 doi:10.1074/jbc.275.6.3873

[2] Dutta SJ, Liu J, Stemmler AJ, Mitra B. Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: effect on metal selectivity and activity. Biochemistry. 2007 Mar 27;46(12):3692-703. PMID:17326661 doi:10.1021/bi0616394

[3] Beard SJ, Hashim R, Membrillo-Hernández J, Hughes MN, Poole RK. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol Microbiol. 1997 Sep;25(5):883-91. PMID:9364914 doi:10.1111/j.1365-2958.1997.mmi518.x

[4] Rensing C, Mitra B, Rosen BP. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14326-31. PMID:9405611 doi:10.1073/pnas.94.26.14326

[5] Rensing C, Sun Y, Mitra B, Rosen BP. Pb(II)-translocating P-type ATPases. J Biol Chem. 1998 Dec 4;273(49):32614-7. PMID:9830000 doi:10.1074/jbc.273.49.32614

[6] Banci L, Bertini I, Ciofi-Baffoni S, Finney LA, Outten CE, O'Halloran TV. 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. 2002 Nov 8;323(5):883-97. PMID:12417201

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