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TitleStructure and conformational variability of the mycobacterium tuberculosis fatty acid synthase multienzyme complex.
Journal, issue, pagesStructure, Vol. 21, Issue 7, Page 1251-1257, Year 2013
Publish dateJul 2, 2013
AuthorsLuciano Ciccarelli / Sean R Connell / Mathias Enderle / Deryck J Mills / Janet Vonck / Martin Grininger /
PubMed AbstractAntibiotic therapy in response to Mycobacterium tuberculosis infections targets de novo fatty acid biosynthesis, which is orchestrated by a 1.9 MDa type I fatty acid synthase (FAS). Here, we ...Antibiotic therapy in response to Mycobacterium tuberculosis infections targets de novo fatty acid biosynthesis, which is orchestrated by a 1.9 MDa type I fatty acid synthase (FAS). Here, we characterize M. tuberculosis FAS by single-particle cryo-electron microscopy and interpret the data by docking the molecular models of yeast and Mycobacterium smegmatis FAS. Our analysis reveals a porous barrel-like structure of considerable conformational variability that is illustrated by the identification of several conformational states with altered topology in the multienzymatic assembly. This demonstrates that the barrel-like structure of M. tuberculosis FAS is not just a static scaffold for the catalytic domains, but may play an active role in coordinating fatty acid synthesis. The conception of M. tuberculosis FAS as a highly dynamic assembly of domains revises the view on bacterial type I fatty acid synthesis and might inspire new strategies for inhibition of de novo fatty acid synthesis in M. tuberculosis.
External linksStructure / PubMed:23746808
MethodsEM (single particle)
Resolution17.5 - 27.0 Å
Structure data

2357

4v8w

EMDB-2357, PDB-4v8w:
Structure and conformational variability of the Mycobacterium tuberculosis fatty acid synthase multienzyme complex
Method: EM (single particle) / Resolution: 17.5 Å

2358

4v8v

EMDB-2358, PDB-4v8v:
Structure and conformational variability of the Mycobacterium tuberculosis fatty acid synthase multienzyme complex
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-2359:
Structure and conformational variability of the Mycobacterium tuberculosis fatty acid synthase multienzyme complex
Method: EM (single particle) / Resolution: 27.0 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / CODIMENSIONAL PRINCIPAL COMPONENT ANALYSIS / FATTY ACID SYNTHESIS / SAMPLE HETEROGENEITY / PROTEIN FLEXIBILITY

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