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Title7.5-Å cryo-em structure of the mycobacterial fatty acid synthase.
Journal, issue, pagesJ Mol Biol, Vol. 425, Issue 5, Page 841-849, Year 2013
Publish dateMar 11, 2013
AuthorsDaniel Boehringer / Nenad Ban / Marc Leibundgut /
PubMed AbstractThe mycobacterial fatty acid synthase (FAS) complex is a giant 2.0-MDa α(6) homohexameric multifunctional enzyme that catalyzes synthesis of fatty acid precursors of mycolic acids, which are major ...The mycobacterial fatty acid synthase (FAS) complex is a giant 2.0-MDa α(6) homohexameric multifunctional enzyme that catalyzes synthesis of fatty acid precursors of mycolic acids, which are major components of the cell wall in Mycobacteria and play an important role in pathogenicity. Here, we present a three-dimensional reconstruction of the Mycobacterium smegmatis FAS complex at 7.5Å, highly homologous to the Mycobacterium tuberculosis multienzyme, by cryo-electron microscopy. Based on the obtained structural data, which allowed us to identify secondary-structure elements, and sequence homology with the fungal FAS, we generated an accurate architectural model of the complex. The FAS system from Mycobacteria resembles a minimized version of the fungal FAS with much larger openings in the reaction chambers. These architectural features of the mycobacterial FAS may be important for the interaction with mycolic acid processing and condensing enzymes that further modify the precursors produced by FAS and for autoactivation of the FAS complex.
External linksJ Mol Biol / PubMed:23291528
MethodsEM (single particle)
Resolution7.5 Å
Structure data

2238

4v8l

EMDB-2238, PDB-4v8l:
Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase
Method: EM (single particle) / Resolution: 7.5 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

Source
  • mycobacterium smegmatis (bacteria)
KeywordsTRANSFERASE / MYCOLIC ACID BIOSYNTHESIS / MULTIFUNCTIONAL ENZYME / SUBSTRATE CHANNELING

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