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 () and Ron Diskin ()
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Nadav Elad: Weizmann Institute of Science
Szilvia Baron: Weizmann Institute of Science
Yoav Peleg: Weizmann Institute of Science
Shira Albeck: Weizmann Institute of Science
Jacob Grunwald: Weizmann Institute of Science
Gal Raviv: Weizmann Institute of Science
Zippora Shakked: Weizmann Institute of Science
Oren Zimhony: Hebrew University
Ron Diskin: Weizmann Institute of Science

Nature Communications, 2018, vol. 9, issue 1, 1-6

Abstract: Abstract Tuberculosis (TB) is a devastating and rapidly spreading disease caused by Mycobacterium tuberculosis (Mtb). Therapy requires prolonged treatment with a combination of multiple agents and interruptions in the treatment regimen result in emergence and spread of multi-drug resistant (MDR) Mtb strains. MDR Mtb poses a significant global health problem, calling for urgent development of novel drugs to combat TB. Here, we report the 3.3 Å resolution structure of the ~2 MDa type-I fatty acid synthase (FAS-I) from Mtb, determined by single particle cryo-EM. Mtb FAS-I is an essential enzymatic complex that contributes to the virulence of Mtb, and thus a prime target for anti-TB drugs. The structural information for Mtb FAS-I we have obtained enables computer-based drug discovery approaches, and the resolution achieved by cryo-EM is sufficient for elucidating inhibition mechanisms by putative small molecular weight inhibitors.

Date: 2018
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DOI: 10.1038/s41467-018-06440-6

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