date: 2015-10-29T13:18:41Z
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pdf:docinfo:title: Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
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dc:description: 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 A resolution.
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description: 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 A resolution.
dcterms:created: 2015-10-23T12:00:00Z
Last-Modified: 2015-10-29T13:18:41Z
dcterms:modified: 2015-10-29T13:18:41Z
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title: Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
Last-Save-Date: 2015-10-29T13:18:41Z
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dc:title: Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
modified: 2015-10-29T13:18:41Z
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created: 2015-10-23T12:00:00Z
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producer: International Union of Crystallography
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pdf:docinfo:producer: International Union of Crystallography
pdf:docinfo:created: 2015-10-23T12:00:00Z