2GPW
Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.
Summary for 2GPW
| Entry DOI | 10.2210/pdb2gpw/pdb |
| Related | 1bnc 1dv1 1dv2 1w93 1w96 |
| Descriptor | Biotin carboxylase (2 entities in total) |
| Functional Keywords | atp-grasp, carboxylase, biotin-dependent, fatty acid synthesis, dimer-interface mutant, ligase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 205927.69 |
| Authors | Shen, Y.,Chou, C.Y.,Chang, G.G.,Tong, L. (deposition date: 2006-04-18, release date: 2006-07-04, Last modification date: 2023-08-30) |
| Primary citation | Shen, Y.,Chou, C.Y.,Chang, G.G.,Tong, L. Is dimerization required for the catalytic activity of bacterial biotin carboxylase? Mol.Cell, 22:807-818, 2006 Cited by PubMed Abstract: Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid metabolism. The biotin carboxylase (BC) subunit of Escherichia coli ACC is believed to be active only as a dimer, although the crystal structure shows that the active site of each monomer is 25 A from the dimer interface. We report here biochemical, biophysical, and structural characterizations of BC carrying single-site mutations in the dimer interface. Our studies demonstrate that two of the mutants, R19E and E23R, are monomeric in solution but have only a 3-fold loss in catalytic activity. The crystal structures of the E23R and F363A mutants show that they can still form the correct dimer at high concentrations. Our data suggest that dimerization is not an absolute requirement for the catalytic activity of the E. coli BC subunit, and we propose a new model for the molecular mechanism of action for BC in multisubunit and multidomain ACCs. PubMed: 16793549DOI: 10.1016/j.molcel.2006.04.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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