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

ABSTRACT: 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.

SUBMITTER: Enderle M

PROVIDER: S-EPMC4631590 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

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

Enderle Mathias M McCarthy Andrew A Paithankar Karthik Shivaji KS Grininger Martin M

Acta crystallographica. Section F, Structural biology communications 20151023 Pt 11

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 pro ...[more]

PMID: 26527268

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