Gating mechanism of elongating β-ketoacyl-ACP synthases

Jeffrey T. Mindrebo; Ashay Patel; Woojoo E. Kim; Tony D. Davis; Aochiu Chen; Thomas G. Bartholow; James J. La Clair; J. Andrew McCammon; Joseph P. Noel; Michael D. Burkart

doi:10.1038/s41467-020-15455-x

Nature Communications (Apr 2020)

Gating mechanism of elongating β-ketoacyl-ACP synthases

Jeffrey T. Mindrebo,
Ashay Patel,
Woojoo E. Kim,
Tony D. Davis,
Aochiu Chen,
Thomas G. Bartholow,
James J. La Clair,
J. Andrew McCammon,
Joseph P. Noel,
Michael D. Burkart

Affiliations

Jeffrey T. Mindrebo: Department of Chemistry and Biochemistry, University of California
Ashay Patel: Department of Chemistry and Biochemistry, University of California
Woojoo E. Kim: Department of Chemistry and Biochemistry, University of California
Tony D. Davis: Department of Chemistry and Biochemistry, University of California
Aochiu Chen: Department of Chemistry and Biochemistry, University of California
Thomas G. Bartholow: Department of Chemistry and Biochemistry, University of California
James J. La Clair: Department of Chemistry and Biochemistry, University of California
J. Andrew McCammon: Department of Chemistry and Biochemistry, University of California
Joseph P. Noel: Department of Chemistry and Biochemistry, University of California
Michael D. Burkart: Department of Chemistry and Biochemistry, University of California

DOI: https://doi.org/10.1038/s41467-020-15455-x
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 15

Abstract

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The formation of C-C bonds in fatty acid and polyketide biosynthesis depends on β-ketoacyl-acyl carrier protein (ACP) synthases (KSs). Here, the authors present structures of E.coli KSs bound to substrate mimetic bearing ACPs, providing insights into the catalytic mechanism underlying C-C bond forming reactions.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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