1OQ6

solution structure of Copper-S46V CopA from Bacillus subtilis

Summary for 1OQ6

• Entry DOI: 10.2210/pdb1oq6/pdb
• Related: 1OPZ 1OQ3
• NMR Information: BMRB: 5768
• Descriptor: Potential copper-transporting ATPase, COPPER (II) ION (2 entities in total)
• Functional Keywords: p-type atpase, mutation, folding, copper complex, structural proteomics in europe, spine, structural genomics, hydrolase
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane; Multi-pass membrane protein: O32220
• Total number of polymer chains: 1
• Total formula weight: 8237.98

Authors

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gonnelli, l.,Su, X.C.,Structural Proteomics in Europe (SPINE) (deposition date: 2003-03-07, release date: 2003-09-16, Last modification date: 2024-05-22)

Primary citation

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gonnelli, l.,Su, X.C.
A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis
J.Mol.Biol., 331:473-484, 2003

PubMed Abstract: 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.

PubMed: 12888353
DOI: 10.1016/S0022-2836(03)00769-1

Experimental method

SOLUTION NMR