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Article

The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin.

Journal of molecular biology - 4 May 2007

Roos Goedele, Garcia-Pino Abel, Van Belle Karolien, Brosens Elke, Wahni Khadija, Vandenbussche Guy, Wyns Lode, Loris Remy, Messens Joris

Abstract excerpt

Nature uses thioredoxin-like folds in several disulfide bond oxidoreductases. Each of them has a typical active site Cys-X-X-Cys sequence motif, the hallmark of thioredoxin being Trp-Cys-Gly-Pro-Cys. The intriguing role of the highly conserved proline in the ubiquitous reducing agent thioredoxin was studied by site-specific mutagenesis of Staphylococcus aureus thioredoxin (Sa_Trx). We present X-ray structures,...

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Identifiers

PMID: 17368484
DOI: 10.1016/j.jmb.2007.02.045

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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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