2KOS
NMR solution structures of octanoyl-ACP from Streptomyces coelicolor Fatty Acid Synthase
Summary for 2KOS
| Entry DOI | 10.2210/pdb2kos/pdb |
| Related | 2kOO 2kOP 2kOQ 2kOR |
| NMR Information | BMRB: 16528 |
| Descriptor | Acyl carrier protein, S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] octanethioate (2 entities in total) |
| Functional Keywords | acyl carrier protein, intermediate binding, fatty acid synthase, transport protein |
| Biological source | Streptomyces coelicolor |
| Cellular location | Cytoplasm (By similarity): P72393 |
| Total number of polymer chains | 1 |
| Total formula weight | 9278.32 |
| Authors | Ploskon, E.,Arthur, C.,Crump, M.P. (deposition date: 2009-09-29, release date: 2010-08-18, Last modification date: 2024-10-30) |
| Primary citation | Ploskon, E.,Arthur, C.J.,Kanari, A.L.,Wattana-amorn, P.,Williams, C.,Crosby, J.,Simpson, T.J.,Willis, C.L.,Crump, M.P. Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis Chem.Biol., 17:776-785, 2010 Cited by PubMed Abstract: It remains unclear whether in a bacterial fatty acid synthase (FAS) acyl chain transfer is a programmed or diffusion controlled and random action. Acyl carrier protein (ACP), which delivers all intermediates and interacts with all synthase enzymes, is the key player in this process. High-resolution structures of intermediates covalently bound to an ACP representing each step in fatty acid biosynthesis have been solved by solution NMR. These include hexanoyl-, 3-oxooctanyl-, 3R-hydroxyoctanoyl-, 2-octenoyl-, and octanoyl-ACP from Streptomyces coelicolor FAS. The high-resolution structures reveal that the ACP adopts a unique conformation for each intermediate driven by changes in the internal fatty acid binding pocket. The binding of each intermediate shows conserved structural features that may ensure effective molecular recognition over subsequent rounds of fatty acid biosynthesis. PubMed: 20659690DOI: 10.1016/j.chembiol.2010.05.024 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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