6RIW
PfaC Keto synthase-Chain length factor
Summary for 6RIW
| Entry DOI | 10.2210/pdb6riw/pdb |
| Descriptor | ORF10, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | pufa synthase, pks synthase, ketosynthase, chain length factor |
| Biological source | Moritella marina |
| Total number of polymer chains | 1 |
| Total formula weight | 108352.04 |
| Authors | Santin, O.,Moncalian, G. (deposition date: 2019-04-25, release date: 2020-08-26, Last modification date: 2024-01-24) |
| Primary citation | Santin, O.,Yuet, K.,Khosla, C.,Moncalian, G. Structure and Mechanism of the Ketosynthase-Chain Length Factor Didomain from a Prototypical Polyunsaturated Fatty Acid Synthase. Biochemistry, 59:4735-4743, 2020 Cited by PubMed Abstract: Long-chain polyunsaturated fatty acids (LC-PUFAs) are essential ingredients of the human diet. They are synthesized by LC-PUFA synthases (PFASs) expressed in marine bacteria and other organisms. PFASs are large enzyme complexes that are homologous to mammalian fatty acid synthases and microbial polyketide synthases. One subunit of each PFAS harbors consecutive ketosynthase (KSc) and chain length factor (CLF) domains that collectively catalyze the elongation of a nascent fatty acyl chain via iterative carbon-carbon bond formation. We report the X-ray crystal structure of the KS-CLF didomain from a well-studied PFAS in . Our structure, in combination with biochemical analysis, provides a foundation for understanding the mechanism of substrate recognition and chain length control by the KS-CLF didomain as well as its interaction with a cognate acyl carrier protein partner. PubMed: 33283513DOI: 10.1021/acs.biochem.0c00785 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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