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.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology