2aj1: Difference between revisions

Revision as of 15:34, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2aj1.png

Template:STRUCTURE 2aj1

Solution structure of apoCadASolution structure of apoCadA

Template:ABSTRACT PUBMED 16388822

About this StructureAbout this Structure

2AJ1 is a Single protein structure of sequence from Listeria monocytogenes. Full experimental 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 Tue Jul 29 15:34:53 2008

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OCA

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 {{STRUCTURE_2aj1|  PDB=2aj1  |  SCENE=  }}
-'''Solution structure of apoCadA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16388822}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16388822 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16388822}}
 ==About this Structure==
-AJ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJ1 OCA].
+AJ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJ1 OCA].
 ==Reference==
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 [[Category: Ferrodoxin-like fold]]
 [[Category: Metal binding protein]]
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