Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex

The Escherichia coli pyruvate dehydrogenase multienzyme complex contains multiple copies of three enzymatic components, E1p, E2p, and E3, that sequentially carry out distinct steps in the overall reaction converting pyruvate to acetyl-CoA. Efficient functioning requires the enzymatic components to a...

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Autores principales: Arjunan, Palaniappa, Wang, Junjie, Nemeria, Natalia S., Reynolds, Shelley, Brown, Ian, Chandrasekhar, Krishnamoorthy, Calero, Guillermo, Jordan, Frank, Furey, William
Formato: Artigo
Lenguaje:Inglês
Publicado: American Society for Biochemistry and Molecular Biology 2014
Materias:
Enzymology
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC4208021/
https://ncbi.nlm.nih.gov/pubmed/25210042
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.592915
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