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Title | Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution. |
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Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 3886, Year 2018 |
Publish date | Sep 24, 2018 |
Authors | Nadav Elad / Szilvia Baron / Yoav Peleg / Shira Albeck / Jacob Grunwald / Gal Raviv / Zippora Shakked / Oren Zimhony / Ron Diskin / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:30250274 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 Å |
Structure data | |
Chemicals | ChemComp-FMN: |
Source |
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Keywords | BIOSYNTHETIC PROTEIN / Fatty Acid Synthesis / Tuberculosis |