Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex

Junjie Wang, Natalia S. Nemeria, Krishnamoorthy Chandrasekhar, Sowmini Kumaran, Palaniappa Arjunan, Shelley Reynolds, Guillermo Calero, Roman Brukh, Lazaros Kakalis, William Furey, Frank Jordan

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Background: The E. coli pyruvate dehydrogenase complex catalyzes conversion of pyruvate to acetyl-CoA and comprises E1p, E2p, and E3 components. Results: The structure of the E2 core domain was solved and shown to efficiently catalyze acetyl transfer between domains. Conclusion: Mass spectrometry revealed hitherto unrecognized domain-induced interactions between E1 and E2 core domain. Significance: A multifaceted approach is required to understand communication between intact multidomain components.

Original languageEnglish (US)
Pages (from-to)15215-15230
Number of pages16
JournalJournal of Biological Chemistry
Volume289
Issue number22
DOIs
StatePublished - May 30 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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