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

Enderle, Mathias; McCarthy, Andrew; Grininger, Martin

doi:10.1107/S2053230X15018336

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

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Abstract

Bacterial and fungal type I fatty-acid synthases (FAS I) are evolutionarily connected, as bacterial FAS I is considered to be the ancestor of fungal FAS I. In this work, the production, crystallization and X-ray diffraction data analysis of a bacterial FAS I are reported. 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.

Authors:

Enderle, Mathias ^[1]; McCarthy, Andrew ^[2]; Grininger, Martin ^[1]

Goethe University Frankfurt, Max-von-Laue-Strasse 15, 60438 Frankfurt am Main (Germany)
EMBL Grenoble, 71 Avenue des Martyrs, 38042 Grenoble CEDEX 9 (France)

Publication Date:: Fri Oct 23 00:00:00 EDT 2015

OSTI Identifier:: 22515176

Resource Type:: Journal Article

Journal Name:: Acta Crystallographica. Section F, Structural Biology Communications

Additional Journal Information:: Journal Volume: 71; Journal Issue: Pt 11; Other Information: PMCID: PMC4631590; PMID: 26527268; PUBLISHER-ID: no5090; PUBLISHER-ID: S2053230X15018336; OAI: oai:pubmedcentral.nih.gov:4631590; Copyright (c) Enderle et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 2053-230X

Country of Publication:: United States

Language:: English

Subject:: 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; DATA ANALYSIS; X RADIATION; X-RAY DIFFRACTION

Citation Formats


                    Enderle, Mathias, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, McCarthy, Andrew, Paithankar, Karthik Shivaji, E-mail: paithankar@em.uni-frankfurt.de, Grininger, Martin, and Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried. Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I.  United States: N. p., 2015. 
        Web.  doi:10.1107/S2053230X15018336.

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                    Enderle, Mathias, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, McCarthy, Andrew, Paithankar, Karthik Shivaji, E-mail: paithankar@em.uni-frankfurt.de, Grininger, Martin, & Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried. Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I.  United States.  https://doi.org/10.1107/S2053230X15018336

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                    Enderle, Mathias, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, McCarthy, Andrew, Paithankar, Karthik Shivaji, E-mail: paithankar@em.uni-frankfurt.de, Grininger, Martin, and Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried. 2015.  
        "Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I".  United States.  https://doi.org/10.1107/S2053230X15018336.

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@article{osti_22515176,

  title        = {Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I},

  author       = {Enderle, Mathias and Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried and McCarthy, Andrew and Paithankar, Karthik Shivaji, E-mail: paithankar@em.uni-frankfurt.de and Grininger, Martin and Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried},

  abstractNote = {Bacterial and fungal type I fatty-acid synthases (FAS I) are evolutionarily connected, as bacterial FAS I is considered to be the ancestor of fungal FAS I. In this work, the production, crystallization and X-ray diffraction data analysis of a bacterial FAS I are reported. 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.},

  doi          = {10.1107/S2053230X15018336},

  url          = {https://www.osti.gov/biblio/22515176},
  journal      = {Acta Crystallographica. Section F, Structural Biology Communications},

  issn         = {2053-230X},

  number       = Pt 11,

  volume       = 71,

  place        = {United States},

  year         = {Fri Oct 23 00:00:00 EDT 2015},

  month        = {Fri Oct 23 00:00:00 EDT 2015}

}

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