Work

Structure and Mechanism of the Ketosynthase-Chain Length Factor Didomain from a Prototypical Polyunsaturated Fatty Acid Synthase

Year: 2020

Type: article

Abstract: Long-chain polyunsaturated fatty acids (LC-PUFA) are essential ingredients of the human diet. They are synthesized by LC-PUFA synthases (PFAS) expressed in marine bacteria and other organisms. PFASs are large enzyme complexes homologous to mammalian fatty acid synthases and microbial polyketide synthases. One subunit of each PFAS harbors consecutive ketosynthase (KS) 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 Moritella marina. Our structure, in combination with biochemical analysis, has provided new insights into substrate recognition and chain length control by the KS-CLF as well as its interaction with a cognate acyl carrier protein partner.

Source: Biochemistry

DOI: 10.1021/acs.biochem.0c00785

Authors: Omar Santín, Kai Yuet, Chaitan Khosla, Gabriel Moncalián

Institutions: Universidad de Cantabria, Instituto de Biomedicina y Biotecnología de Cantabria, Stanford University

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Pharmacology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: Ministerio de Ciencia, Innovación y Universidades, European Regional Development Fund, National Institute of General Medical Sciences

Awards: Structure, Mechanism, and Engineering of Assembly Line Polyketide Synthases, G4376682986, G6036527932, G6743256178, G675104627