5KOF
Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and Acyl Carrier Protein, AcpP
Summary for 5KOF
| Entry DOI | 10.2210/pdb5kof/pdb |
| Descriptor | 3-oxoacyl-[acyl-carrier-protein] synthase 1, Acyl carrier protein, [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-[2-(prop-2-enoylamino)ethylamino]propyl]amino]butyl] dihydrogen phosphate, ... (4 entities in total) |
| Functional Keywords | crosslinked, ketosynthase, acp, complex, transferase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 103536.17 |
| Authors | Milligan, J.C.,Jackson, D.R.,Barajas, J.F.,Tsai, S.C. (deposition date: 2016-06-30, release date: 2018-01-24, Last modification date: 2023-10-04) |
| Primary citation | Milligan, J.C.,Lee, D.J.,Jackson, D.R.,Schaub, A.J.,Beld, J.,Barajas, J.F.,Hale, J.J.,Luo, R.,Burkart, M.D.,Tsai, S.C. Molecular basis for interactions between an acyl carrier protein and a ketosynthase. Nat.Chem.Biol., 15:669-671, 2019 Cited by PubMed Abstract: Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli. PubMed: 31209348DOI: 10.1038/s41589-019-0301-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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