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Article

A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis.

Journal of molecular biology - 8 Aug 2003

Banci Lucia, Bertini Ivano, Ciofi-Baffoni Simone, Gonnelli Leonardo, Su Xun-Cheng

Abstract excerpt

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...

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Identifiers

PMID: 12888353
DOI: 10.1016/s0022-2836(03)00769-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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