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  Structure and Conformational Variability of the Mycobacterium tuberculosis Fatty Acid Synthase Multienzyme Complex

Ciccarelli, L., Connell, S. R., Enderle, M., Mills, D. J., Vonck, J., & Grininger, M. (2013). Structure and Conformational Variability of the Mycobacterium tuberculosis Fatty Acid Synthase Multienzyme Complex. STRUCTURE, 21(7), 1251-1257. doi:10.1016/j.str.2013.04.023.

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 Creators:
Ciccarelli, Luciano1, Author
Connell, Sean R.1, Author              
Enderle, Mathias2, Author              
Mills, Deryck J.1, Author
Vonck, Janet1, Author
Grininger, Martin2, Author              
Affiliations:
1external, ou_persistent22              
2Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

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Free keywords: ACYL-CARRIER PROTEIN; BREVIBACTERIUM-AMMONIAGENES; ELECTRON CRYOMICROSCOPY; CRYSTAL-STRUCTURE; BIOSYNTHESIS; SYNTHETASE; PYRAZINAMIDE; PURIFICATION; FLEXIBILITY; MUTAGENESIS
 Abstract: Antibiotic therapy in response to Mycobacterium tuberculosis infections targets de novo fatty acid biosynthesis, which is orchestrated by a 1.9 MDa type I fatty acid synthase (FAS). Here, we characterize M. tuberculosis FAS by single-particle cryo-electron microscopy and interpret the data by docking the molecular models of yeast and Mycobacterium smegmatis FAS. Our analysis reveals a porous barrel-like structure of considerable conformational variability that is illustrated by the identification of several conformational states with altered topology in the multienzymatic assembly. This demonstrates that the barrel-like structure of M. tuberculosis FAS is not just a static scaffold for the catalytic domains, but may play an active role in coordinating fatty acid synthesis. The conception of M. tuberculosis FAS as a highly dynamic assembly of domains revises the view on bacterial type I fatty acid synthesis and might inspire new strategies for inhibition of de novo fatty acid synthesis in M. tuberculosis.

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Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000321681600022
DOI: 10.1016/j.str.2013.04.023
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 21 (7) Sequence Number: - Start / End Page: 1251 - 1257 Identifier: ISSN: 0969-2126