2aj0: Difference between revisions
New page: left|200px<br /><applet load="2aj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aj0" /> '''Solution structure of apoCadA'''<br /> ==Ov... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2aj0.gif|left|200px]]<br /><applet load="2aj0" size=" | [[Image:2aj0.gif|left|200px]]<br /><applet load="2aj0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2aj0" /> | caption="2aj0" /> | ||
'''Solution structure of apoCadA'''<br /> | '''Solution structure of apoCadA'''<br /> | ||
==Overview== | ==Overview== | ||
In bacteria, P1-type ATPases are responsible for resistance to di- and | 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== | ==About this Structure== | ||
2AJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Active as [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] Full crystallographic information is available from [http:// | 2AJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJ0 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: Mintz, E.]] | [[Category: Mintz, E.]] | ||
[[Category: Miras, R.]] | [[Category: Miras, R.]] | ||
[[Category: Scott, R | [[Category: Scott, R A.]] | ||
[[Category: Shokes, J | [[Category: Shokes, J E.]] | ||
[[Category: Su, X | [[Category: Su, X C.]] | ||
[[Category: beta-alpha-beta-beta-alpha-beta]] | [[Category: beta-alpha-beta-beta-alpha-beta]] | ||
[[Category: ferrodoxin-like fold]] | [[Category: ferrodoxin-like fold]] | ||
[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:57 2008'' | ||
Revision as of 17:28, 21 February 2008
|
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 Thu Feb 21 16:27:57 2008