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Article

Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants.

Scientific reports - 9 Feb 2017

Noguera Martín E, Vazquez Diego S, Ferrer-Sueta Gerardo, Agudelo William A, Howard Eduardo, Rasia Rodolfo M, Manta Bruno, Cousido-Siah Alexandra, Mitschler André, Podjarny Alberto, Santos Javier

Abstract excerpt

Thioredoxin is a ubiquitous small protein that catalyzes redox reactions of protein thiols. Additionally, thioredoxin from E. coli (EcTRX) is a widely-used model for structure-function studies. In a previous paper, we characterized several single-point mutants of the C-terminal helix (CTH) that alter global stability of EcTRX. However, spectroscopic signatures and enzymatic activity for some of these mutants were...

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Identifiers

PMID: 28181556
DOI: 10.1038/srep42343
PMCID: PMC5299410

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CTH

Variants

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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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