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2aj0

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[[Image:2aj0.gif|left|200px]]
[[Image:2aj0.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2aj0 |SIZE=350|CAPTION= <scene name='initialview01'>2aj0</scene>
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The line below this paragraph, containing "STRUCTURE_2aj0", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= cadA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 Listeria monocytogenes])
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|DOMAIN=
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{{STRUCTURE_2aj0| PDB=2aj0 | SCENE= }}
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|RELATEDENTRY=[[2aj1|2AJ1]]
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|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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'''Solution structure of apoCadA'''
'''Solution structure of apoCadA'''
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[[Category: Shokes, J E.]]
[[Category: Shokes, J E.]]
[[Category: Su, X C.]]
[[Category: Su, X C.]]
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[[Category: beta-alpha-beta-beta-alpha-beta]]
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[[Category: Beta-alpha-beta-beta-alpha-beta]]
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[[Category: ferrodoxin-like fold]]
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[[Category: Ferrodoxin-like fold]]
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[[Category: metal binding protein]]
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[[Category: Metal binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:06:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:21 2008''
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Revision as of 16:06, 3 May 2008

Template:STRUCTURE 2aj0

Solution structure of apoCadA


Overview

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 Structure

2AJ0 is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.

Reference

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 Sat May 3 19:06:29 2008

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