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

Enderle, M., McCarthy, A., Paithankar, K. S., & Grininger, M. (2015). Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 71, 1401-1407. doi:10.1107/S2053230X15018336.

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 Creators:
Enderle, Mathias1, Author              
McCarthy, Andrew2, Author
Paithankar, Karthik Shivaji2, Author
Grininger, Martin1, Author              
Affiliations:
1Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              
2external, ou_persistent22              

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Free keywords: MYCOBACTERIUM-TUBERCULOSIS; MOLECULAR-REPLACEMENT; MULTIENZYME COMPLEX; CONDENSING ENZYMES; DATA QUALITY; YEAST; SYSTEM; FAS; SYNTHETASE; MODELfatty-acid synthase; fatty-acid synthesis; multienzyme; tuberculosis; mycolic acid;
 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 angstrom resolution.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000364557700007
DOI: 10.1107/S2053230X15018336
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Title: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Source Genre: Journal
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Publ. Info: 2 ABBEY SQ, CHESTER, CH1 2HU, ENGLAND : INT UNION CRYSTALLOGRAPHY
Pages: - Volume / Issue: 71 Sequence Number: - Start / End Page: 1401 - 1407 Identifier: ISSN: 2053-230X