Structural highlights
4hr7 is a 8 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | EDO, SO4 |
| Related: | 1dv1, 1bdo |
| Gene: | accC, fabG, b3256, JW3224 (Escherichia coli K-12), accB, fabE, b3255, JW3223 (Escherichia coli K-12) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Function
[ACCC_ECOLI] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. [BCCP_ECOLI] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Publication Abstract from PubMed
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 alpha2beta2 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 A. 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.
The Three-Dimensional Structure of the Biotin Carboxylase-Biotin Carboxyl Carrier Protein Complex of E. coli Acetyl-CoA Carboxylase.,Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL Structure. 2013 Mar 12. pii: S0969-2126(13)00041-5. doi:, 10.1016/j.str.2013.02.001. PMID:23499019[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL. The Three-Dimensional Structure of the Biotin Carboxylase-Biotin Carboxyl Carrier Protein Complex of E. coli Acetyl-CoA Carboxylase. Structure. 2013 Mar 12. pii: S0969-2126(13)00041-5. doi:, 10.1016/j.str.2013.02.001. PMID:23499019 doi:10.1016/j.str.2013.02.001
