2aj0: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Cadmium-exporting_ATPase Cadmium-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.3 3.6.3.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cadmium-exporting_ATPase Cadmium-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.3 3.6.3.3] </span> | ||
|GENE= cadA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 Listeria monocytogenes]) | |GENE= cadA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 Listeria monocytogenes]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2aj1|2AJ1]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aj0 OCA], [http://www.ebi.ac.uk/pdbsum/2aj0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aj0 RCSB]</span> | |||
}} | }} | ||
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[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:21 2008'' | ||
Revision as of 01:53, 31 March 2008
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| Gene: | cadA (Listeria monocytogenes) | ||||||
| Activity: | Cadmium-exporting ATPase, with EC number 3.6.3.3 | ||||||
| Related: | 2AJ1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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