P1B-3 型 ATP 酶 CopB 中的跨膜 II 型类似铜 2+ 结合位点：对金属选择性的影响。
Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.
机构信息
Division of Chemistry and Chemical Engineering and ‡Howard Hughes Medical Institute, California Institute of Technology , Pasadena, California 91125, United States of America.
出版信息
ACS Chem Biol. 2014 Jan 17;9(1):116-21. doi: 10.1021/cb400603t. Epub 2013 Nov 1.
Abstract
Metal selectivity in P1B-type ATPase transporters is determined by conserved amino acid residues in their transmembrane helices responsible for metal binding and transport across the cellular membrane. The Cu(2+)-selective CopB from Archaeoglobus fulgidus has been investigated to explore the coordination chemistry of the transition metal binding sites in P1B-3-type ATPases. Electronic absorption, electron paramagnetic resonance, and X-ray absorption spectroscopic studies indicate the presence of a high-affinity transmembrane Type-2-like Cu(2+) center in which a single cupric ion is coordinated in a distorted square pyramidal geometry by mixed nitrogen/oxygen and sulfur ligands.
摘要
金属选择性在 P1B 型 ATP 酶转运体中由其跨细胞膜负责金属结合和转运的跨膜螺旋中的保守氨基酸残基决定。已经研究了来自古生球菌属的 Cu(2+)-选择性 CopB，以探索 P1B-3 型 ATP 酶中过渡金属结合位点的配位化学。电子吸收、电子顺磁共振和 X 射线吸收光谱研究表明，存在一个高亲和力的跨膜 Type-2 样 Cu(2+)中心，其中一个单个的铜离子通过混合氮/氧和硫配体在扭曲的四方锥几何结构中配位。
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1
Characterization of the PIB-Type ATPases present in Thermus thermophilus.
J Bacteriol. 2012 Aug;194(15):4107-13. doi: 10.1128/JB.00849-12. Epub 2012 May 25.
2
P-type ATPases at a glance.
J Cell Sci. 2011 Aug 1;124(Pt 15):2515-9. doi: 10.1242/jcs.088716.
3
Crystal structure of a copper-transporting PIB-type ATPase.
Nature. 2011 Jun 29;475(7354):59-64. doi: 10.1038/nature10191.
4
A spectrophotometric method for the determination of zinc, copper, and cobalt ions in metalloproteins using Zincon.
Anal Biochem. 2010 Feb 15;397(2):218-26. doi: 10.1016/j.ab.2009.10.037. Epub 2009 Oct 23.
5
Crystal structure of the sodium-potassium pump at 2.4 A resolution.
Nature. 2009 May 21;459(7245):446-50. doi: 10.1038/nature07939.
6
TOPCONS: consensus prediction of membrane protein topology.
Nucleic Acids Res. 2009 Jul;37(Web Server issue):W465-8. doi: 10.1093/nar/gkp363. Epub 2009 May 8.
7
Structure of the two transmembrane Cu+ transport sites of the Cu+ -ATPases.
J Biol Chem. 2008 Oct 31;283(44):29753-9. doi: 10.1074/jbc.M803248200. Epub 2008 Sep 4.
8
Membrane structure of CtrA3, a copper-transporting P-type-ATPase from Aquifex aeolicus.
J Mol Biol. 2008 May 2;378(3):581-95. doi: 10.1016/j.jmb.2008.01.094. Epub 2008 Feb 12.
9
Crystal structure of the plasma membrane proton pump.
Nature. 2007 Dec 13;450(7172):1111-4. doi: 10.1038/nature06417.
10
Crystal structure of the sodium-potassium pump.
Nature. 2007 Dec 13;450(7172):1043-9. doi: 10.1038/nature06419.
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