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Article

A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.

Structure (London, England : 1993) - 12 Aug 2009

Stott Katherine M, Yusof Adlina M, Perham Richard N, Jones D Dafydd

Abstract excerpt

A prominent surface loop links the first two beta strands of the lipoyl domain (E2plip) from the pyruvate dehydrogenase multienzyme complex of Escherichia coli. We show here that shortening this loop by two residues generates a protein that populates two structurally distinct stable conformers: an active, native-like monomer (HM) and a functionally compromised misfolded dimer (LM). Conversion of LM to HM was...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 19679089
DOI: 10.1016/j.str.2009.07.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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