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Article

Coupling of domain swapping to kinetic stability in a thioredoxin mutant.

Journal of molecular biology - 6 Feb 2009

Garcia-Pino Abel, Martinez-Rodriguez Sergio, Wahni Khadija, Wyns Lode, Loris Remy, Messens Joris

Abstract excerpt

The thioredoxin (Trx) fold is a small monomeric domain that is ubiquitous in redox-active enzymes. Trxs are characterized by a typical WCGPC active-site sequence motif. A single active-site mutation of the tryptophan to an alanine in Staphylococcus aureus Trx converts the oxidized protein into a biologically inactive domain-swapped dimer. While the monomeric protein unfolds reversibly in a two-state manner, the...

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Identifiers

PMID: 19071139
DOI: 10.1016/j.jmb.2008.11.040

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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