4HR7

Crystal Structure of Biotin Carboxyl Carrier Protein-Biotin Carboxylase Complex from E.coli

Summary for 4HR7

• Entry DOI: 10.2210/pdb4hr7/pdb
• Related: 1BDO 1DV1
• Descriptor: Biotin carboxylase, Biotin carboxyl carrier protein of acetyl-CoA carboxylase, SULFATE ION, ... (5 entities in total)
• Functional Keywords: biotin carboxylase, biotin carboxyl carrier protein, acetyl-coa carboxylase, protein-protein interaction, protein complex, protein interface, antibiotic target, atp grasp, biotin-dependent carboxylase, fatty acid synthesis, ligase-biotin binding protein complex, ligase/biotin binding protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 8
• Total formula weight: 274251.53

Authors

Broussard, T.C.,Kobe, M.J.,Pakhomova, S.,Neau, D.B.,Price, A.E.,Champion, T.S.,Waldrop, G.L. (deposition date: 2012-10-26, release date: 2013-03-13, Last modification date: 2023-09-20)

Primary citation

Broussard, T.C.,Kobe, M.J.,Pakhomova, S.,Neau, D.B.,Price, A.E.,Champion, T.S.,Waldrop, G.L.
The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase.
Structure, 21:650-657, 2013

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.

PubMed: 23499019
DOI: 10.1016/j.str.2013.02.001

Experimental method

X-RAY DIFFRACTION (2.495 Å)