2aj0
Solution structure of apoCadA
|
OverviewOverview
In bacteria, P1-type ATPases are responsible for resistance to di- and, monovalent toxic heavy metals by taking them out of the cell. These, ATPases have a cytoplasmic N terminus comprising metal binding domains, defined by a betaalphabetabetaalphabeta fold and a CXXC metal binding, motif. To check how the structural properties of the metal binding site in, the N terminus can influence the metal specificity of the ATPase, the, first structure of a Cd(II)-ATPase N terminus was determined by NMR and, its coordination sphere was investigated by X-ray absorption spectroscopy., A novel metal binding environment was found, comprising the two conserved, Cys residues of the metal binding motif and a Glu in loop 5. A, bioinformatic search identifies an ensemble of highly homologous sequences, presumably with the same function. Another group of highly homologous, sequences is found which can be referred to as zinc-detoxifying P1-type, ATPases with the metal binding pattern DCXXC in the N terminus. Because no, carboxylate groups participate in Cu(I) or Ag(I) binding sites, we suggest, that the acidic residue plays a key role in the coordination properties of, divalent cations, hence conferring a function to the N terminus in the, metal specificity of the ATPase.
About this StructureAbout this Structure
2AJ0 is a Single protein structure of sequence from Listeria monocytogenes. Active as Cadmium-exporting ATPase, with EC number 3.6.3.3 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA., Banci L, Bertini I, Ciofi-Baffoni S, Su XC, Miras R, Bal N, Mintz E, Catty P, Shokes JE, Scott RA, J Mol Biol. 2006 Feb 24;356(3):638-50. Epub 2005 Dec 5. PMID:16388822
Page seeded by OCA on Wed Nov 21 08:09:27 2007