The Three-Dimensional Structure of the Biotin Carboxylase-Biotin Carboxyl Carrier Protein Complex of E. coli Acetyl-CoA Carboxylase
Autor: | Matthew J. Kobe, Amanda E. Price, Grover L. Waldrop, Svetlana Pakhomova, Tyler S. Champion, David B. Neau, Tyler C. Broussard |
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Rok vydání: | 2013 |
Předmět: |
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Molecular Biotin carboxylase Enzyme complex Protein Conformation Biotin carboxyl carrier protein Biology Article 03 medical and health sciences X-Ray Diffraction Structural Biology Escherichia coli Fatty Acid Synthase Type II Transferase Carbon-Nitrogen Ligases Molecular Biology 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology Acetyl-CoA carboxylase Pyruvate carboxylase Biochemistry Multiprotein Complexes Biotinylation biology.protein Protein quaternary structure Crystallization Acetyl-CoA Carboxylase |
Zdroj: | Structure. 21:650-657 |
ISSN: | 0969-2126 |
Popis: | SummaryAcetyl-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. |
Databáze: | OpenAIRE |
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