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• W2023668832 abstract "<h2>Summary</h2> A prominent surface loop links the first two β strands of the lipoyl domain (E2plip) from the pyruvate dehydrogenase multienzyme complex of <i>Escherichia coli</i>. 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 observed after exposure to temperatures above 50°C. Removal of two additional residues from the loop caused the protein to adopt exclusively the misfolded conformation. Detailed NMR structural studies of the misfolded dimer reveal that the N-terminal half of the domain was unfolded and dynamic, whereas the C-terminal halves of two monomers had associated to form a structure with two-fold symmetry and a topology mimicking that of the folded monomer. The surface loop is therefore a hitherto unsuspected determinant in the folding process that leads to a functional protein." @default.
• W2023668832 created "2016-06-24" @default.
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• W2023668832 date "2009-08-01" @default.
• W2023668832 modified "2023-09-27" @default.
• W2023668832 title "A Surface Loop Directs Conformational Switching of a Lipoyl Domain Between a Folded and a Novel Misfolded Structure" @default.
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• W2023668832 doi "https://doi.org/10.1016/j.str.2009.07.001" @default.
• W2023668832 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19679089" @default.
• W2023668832 hasPublicationYear "2009" @default.
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