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Acta Crystallogr F Struct Biol Commun. 2015 Nov;71(Pt 11):1401-7. doi: 10.1107/S2053230X15018336. Epub 2015 Oct 23.

Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I.

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Institute of Organic Chemistry and Chemical Biology, Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Strasse 15, 60438 Frankfurt am Main, Germany.
EMBL Grenoble, 71 Avenue des Martyrs, 38042 Grenoble CEDEX 9, France.


While a deep understanding of the fungal and mammalian multi-enzyme type I fatty-acid synthases (FAS I) has been achieved in recent years, the bacterial FAS I family, which is narrowly distributed within the Actinomycetales genera Mycobacterium, Corynebacterium and Nocardia, is still poorly understood. This is of particular relevance for two reasons: (i) although homologous to fungal FAS I, cryo-electron microscopic studies have shown that bacterial FAS I has unique structural and functional properties, and (ii) M. tuberculosis FAS I is a drug target for the therapeutic treatment of tuberculosis (TB) and therefore is of extraordinary importance as a drug target. Crystals of FAS I from C. efficiens, a homologue of M. tuberculosis FAS I, were produced and diffracted X-rays to about 4.5 Å resolution.


fatty-acid synthase; fatty-acid synthesis; multienzyme; mycolic acid; tuberculosis

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