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Cryo-EM Structure of the Mycobacterial Fatty Acid SynthaseCryo-EM Structure of the Mycobacterial Fatty Acid Synthase

Structural highlights

4v8l is a 6 chain structure with sequence from Mycobacterium smegmatis. This structure supersedes and combines the now removed PDB entries 4b3y and 3zen. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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Publication Abstract from PubMed

The mycobacterial fatty acid synthase (FAS) complex is a giant 2.0-MDa alpha(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 7.5A, 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.

7.5-A Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase.,Boehringer D, Ban N, Leibundgut M J Mol Biol. 2013 Jan 3. pii: S0022-2836(12)00969-2. doi:, 10.1016/j.jmb.2012.12.021. PMID:23291528[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Boehringer D, Ban N, Leibundgut M. 7.5-A Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase. J Mol Biol. 2013 Jan 3. pii: S0022-2836(12)00969-2. doi:, 10.1016/j.jmb.2012.12.021. PMID:23291528 doi:http://dx.doi.org/10.1016/j.jmb.2012.12.021

4v8l, resolution 7.50Å

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