Summary for 1HN9
| Entry DOI | 10.2210/pdb1hn9/pdb |
| Related | 1hnd 1hnh 1hnj 1hnk |
| Descriptor | BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | fabh, transferase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P0A6R0 |
| Total number of polymer chains | 2 |
| Total formula weight | 67284.00 |
| Authors | Qiu, X.,Janson, C.A.,Konstantinidis, A.K.,Nwagwu, S.,Silverman, C.,Smith, W.W.,Khandekar, S.K.,Lonsdale, J.,Abdel-Meguid, S.S. (deposition date: 2000-12-07, release date: 2000-12-27, Last modification date: 2024-04-03) |
| Primary citation | Qiu, X.,Janson, C.A.,Konstantinidis, A.K.,Nwagwu, S.,Silverman, C.,Smith, W.W.,Khandekar, S.,Lonsdale, J.,Abdel-Meguid, S.S. Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis. J.Biol.Chem., 274:36465-36471, 1999 Cited by PubMed Abstract: Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent member of the family of condensing enzymes, is a key catalyst in bacterial fatty acid biosynthesis and a promising target for novel antibiotics. We report here the crystal structures of FabH determined in the presence and absence of acetyl-CoA. These structures display a fold that is common for condensing enzymes. The observed acetylation of Cys(112) proves its catalytic role and clearly defines the primer binding pocket. Modeling based on a bound CoA molecule suggests catalytic roles for His(244) and Asn(274). The structures provide the molecular basis for FabH substrate specificity and reaction mechanism and are important for structure-based design of novel antibiotics. PubMed: 10593943DOI: 10.1074/jbc.274.51.36465 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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