4V8L

Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase

This is a non-PDB format compatible entry.

Summary for 4V8L

• Entry DOI: 10.2210/pdb4v8l/pdb
• EMDB information: 2238
• Descriptor: FATTY ACID SYNTHASE, FLAVIN MONONUCLEOTIDE (2 entities in total)
• Functional Keywords: transferase, mycolic acid biosynthesis, multifunctional enzyme, substrate channeling
• Biological source: MYCOBACTERIUM SMEGMATIS
• Total number of polymer chains: 6
• Total formula weight: 1957287.56

Authors

Boehringer, D.,Ban, N.,Leibundgut, M. (deposition date: 2012-12-06, release date: 2014-07-09, Last modification date: 2024-05-08)

Primary citation

Boehringer, D.,Ban, N.,Leibundgut, M.
7.5-A Cryo-Em Structure of the Mycobacterial Fatty Acid Synthase.
J.Mol.Biol., 425:841-, 2013

PubMed Abstract: 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.

PubMed: 23291528
DOI: 10.1016/J.JMB.2012.12.021

Experimental method

ELECTRON MICROSCOPY (7.5 Å)