1oq6: Difference between revisions
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{{STRUCTURE_1oq6| PDB=1oq6 | SCENE= }} | |||
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'''solution structure of Copper-S46V CopA from Bacillus subtilis''' | '''solution structure of Copper-S46V CopA from Bacillus subtilis''' | ||
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[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Su, X C.]] | [[Category: Su, X C.]] | ||
[[Category: | [[Category: Copper complex]] | ||
[[Category: | [[Category: Folding]] | ||
[[Category: | [[Category: Mutation]] | ||
[[Category: | [[Category: Nmr]] | ||
[[Category: | [[Category: P-type atpase]] | ||
[[Category: | [[Category: Spine]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Structural proteomics in europe]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:08:56 2008'' | |||
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Revision as of 08:08, 13 April 2008
solution structure of Copper-S46V CopA from Bacillus subtilis
OverviewOverview
The two N-terminal domains of the P-type copper ATPase, CopAa and CopAb, from Bacillus subtilis differ in their folding capabilities in vitro. Whereas CopAb has the typical betaalphabetabetaalphabeta structure and is a rigid protein, CopAa is found to be largely unfolded. A sequence analysis of the two and of orthologue homologous proteins indicates that Ser46 in CopAa may destabilise the hydrophobic core, as also confirmed through a bioinformatic energy study. CopAb has a Val in the corresponding position. The S46V and S46A mutants are found to be folded, although the latter displays multiple conformations. S46VCopAa, in both apo and copper(I) loaded forms, has very similar structural and dynamic properties with respect to CopAb, besides a different length of strand beta2 and beta4. It is intriguing that the oxygen of Thr16 is found close, though at longer than bonding distance, to copper in both domains, as it also occurs in a human orthologue domain. This study contributes to understanding the behaviour of proteins that do not properly fold in vitro. A possible biological significance of the peculiar folding behaviour of this domain is discussed.
About this StructureAbout this Structure
1OQ6 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
ReferenceReference
A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis., Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC, J Mol Biol. 2003 Aug 8;331(2):473-84. PMID:12888353 Page seeded by OCA on Sun Apr 13 08:08:56 2008