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

  • 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.

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Author:Mathias Enderle, Andrew McCarthyORCiD, Karthik Shivaji PaithankarORCiDGND, Martin GriningerORCiDGND
Pubmed Id:
Parent Title (English):Acta crystallographica / Section F, Structural biology communications
Place of publication:Oxford [u.a.]
Document Type:Article
Date of Publication (online):2016/11/09
Date of first Publication:2015/10/23
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2016/11/09
Tag:fatty-acid synthase; fatty-acid synthesis; multienzyme; mycolic acid; tuberculosis
Issue:Pt 11
Page Number:7
First Page:1401
Last Page:1407
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Exzellenzcluster / Exzellenzcluster Makromolekulare Komplexe
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - Namensnennung 4.0