1F91
BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I IN COMPLEX WITH C10 FATTY ACID SUBSTRATE
Summary for 1F91
Entry DOI | 10.2210/pdb1f91/pdb |
Related | 1DD8 1EK4 |
Descriptor | BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I, HYDROXIDE ION, DECANOIC ACID, ... (4 entities in total) |
Functional Keywords | thiolase fold family, dimer, transferase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A953 |
Total number of polymer chains | 4 |
Total formula weight | 171429.85 |
Authors | Olsen, J.G.,Kadziola, A.,Wettstein-Knowles, P.V.,Siggaard-Andersen, M.,Larsen, S. (deposition date: 2000-07-06, release date: 2001-04-11, Last modification date: 2021-11-03) |
Primary citation | Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Larsen, S. Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Structure, 9:233-243, 2001 Cited by PubMed Abstract: beta-ketoacyl-acyl carrier protein synthase (KAS) I is vital for the construction of the unsaturated fatty acid carbon skeletons characterizing E. coli membrane lipids. The new carbon-carbon bonds are created by KAS I in a Claisen condensation performed in a three-step enzymatic reaction. KAS I belongs to the thiolase fold enzymes, of which structures are known for five other enzymes. PubMed: 11286890DOI: 10.1016/S0969-2126(01)00583-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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