Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution

Nadav Elad; Szilvia Baron; Yoav Peleg; Shira Albeck; Jacob Grunwald; Gal Raviv; Zippora Shakked; Oren Zimhony; Ron Diskin

doi:10.1038/s41467-018-06440-6

Nature Communications (Sep 2018)

Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution

Nadav Elad,
Szilvia Baron,
Yoav Peleg,
Shira Albeck,
Jacob Grunwald,
Gal Raviv,
Zippora Shakked,
Oren Zimhony,
Ron Diskin

Affiliations

Nadav Elad: Department of Chemical Research Support, Weizmann Institute of Science
Szilvia Baron: Department of Structural Biology, Weizmann Institute of Science
Yoav Peleg: Structural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science
Shira Albeck: Structural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science
Jacob Grunwald: Structural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science
Gal Raviv: Department of Structural Biology, Weizmann Institute of Science
Zippora Shakked: Department of Structural Biology, Weizmann Institute of Science
Oren Zimhony: Kaplan Medical Center, Rehovot, affiliated to the School of Medicine, Hebrew University
Ron Diskin: Department of Structural Biology, Weizmann Institute of Science

DOI: https://doi.org/10.1038/s41467-018-06440-6
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 6

Abstract

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The type-I fatty acid synthase (FAS-I) complex is essential for Mycobacterium tuberculosis (Mtb) and mediates the production of C26 fatty acids that are precursors for the synthesis of mycolic acids. Here the authors present the 3.3 Å resolution cryo-EM structure of Mtb FAS-I, which is of interest for tuberculosis drug development.

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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