Structural highlights
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.
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
