Structural highlights
Function
COPZ_ARCFU Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) directly to the transmembrane transport sites of copper-exporting P-type ATPase A (CopA). Probably has a redox function due to the presence of a 2Fe-2S cluster and could reduce Cu(2+) to Cu(+).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Arguello JM, Rosenzweig AC. Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus. J Biol Chem. 2007 Aug 31;282(35):25950-9. Epub 2007 Jul 3. PMID:17609202 doi:10.1074/jbc.M703311200
- ↑ Gonzalez-Guerrero M, Arguello JM. Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites. Proc Natl Acad Sci U S A. 2008 Apr 22;105(16):5992-7. Epub 2008 Apr 15. PMID:18417453 doi:http://dx.doi.org/0711446105
