1p6t: Difference between revisions
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'''Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis'''<br /> | '''Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis'''<br /> | ||
==Overview== | ==Overview== | ||
The solution structure of the N-terminal region (151 amino acids) of a | The solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases. | ||
==About this Structure== | ==About this Structure== | ||
1P6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] Full crystallographic information is available from [http:// | 1P6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6T OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ciofi-Baffoni, S.]] | [[Category: Ciofi-Baffoni, S.]] | ||
[[Category: Gonnelli, L.]] | [[Category: Gonnelli, L.]] | ||
[[Category: SPINE, Structural | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Su, X | [[Category: Su, X C.]] | ||
[[Category: copa; p-type atpase; water-soluble region; beta-alpha-beta-beta-alpha-beta fold; nmr]] | [[Category: copa; p-type atpase; water-soluble region; beta-alpha-beta-beta-alpha-beta fold; nmr]] | ||
[[Category: spine]] | [[Category: spine]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:42 2008'' | ||
Revision as of 15:25, 21 February 2008
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Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis
OverviewOverview
The solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases.
About this StructureAbout this Structure
1P6T is a Single protein structure of sequence from Bacillus subtilis. Active as Copper-exporting ATPase, with EC number 3.6.3.4 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis., Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC, J Biol Chem. 2003 Dec 12;278(50):50506-13. Epub 2003 Sep 27. PMID:14514665
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OCA- Pages with broken file links
- Bacillus subtilis
- Copper-exporting ATPase
- Single protein
- Banci, L.
- Bertini, I.
- Ciofi-Baffoni, S.
- Gonnelli, L.
- SPINE, Structural Proteomics in Europe.
- Su, X C.
- Copa; p-type atpase; water-soluble region; beta-alpha-beta-beta-alpha-beta fold; nmr
- Spine
- Structural genomics
- Structural proteomics in europe