Download MendeleyThe three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase.
Broussard, T.C., Kobe, M.J., Pakhomova, S., Neau, D.B., Price, A.E., Champion, T.S., Waldrop, G.L.(2013) Structure 21: 650-657
- PubMed: 23499019
- DOI: https://doi.org/10.1016/j.str.2013.02.001
- Primary Citation of Related Structures:
4HR7 - PubMed Abstract:
Acetyl-coenzyme A (acetyl-CoA) carboxylase is a biotin-dependent, multifunctional enzyme that catalyzes the regulated step in fatty acid synthesis. The Escherichia coli enzyme is composed of a homodimeric biotin carboxylase (BC), biotinylated biotin carboxyl carrier protein (BCCP), and an α2β2 heterotetrameric carboxyltransferase. This enzyme complex catalyzes two half-reactions to form malonyl-coenzyme A. BC and BCCP participate in the first half-reaction, whereas carboxyltransferase and BCCP are involved in the second. Three-dimensional structures have been reported for the individual subunits; however, the structural basis for how BCCP reacts with the carboxylase or transferase is unknown. Therefore, we report here the crystal structure of E. coli BCCP complexed with BC to a resolution of 2.49 Å. The protein-protein complex shows a unique quaternary structure and two distinct interfaces for each BCCP monomer. These BCCP binding sites are unique compared to phylogenetically related biotin-dependent carboxylases and therefore provide novel targets for developing antibiotics against bacterial acetyl-CoA carboxylase.
Organizational Affiliation:
Division of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, LA 70803, USA.
