ArticleActa crystallographica. Section F, Structural biology communications2015
Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).Scientific reports · 2020Article
- Probing the modularity of megasynthases by rational engineering of a fatty acid synthase Type I.Protein science : a publication of the Protein Society · 2019Article
- Expression of a recombinant, 4'-Phosphopantetheinylated, active M. tuberculosis fatty acid synthase I in E. coli.PloS one · 2018Article
- Active Multienzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis.Journal of bacteriology · 2017Article
- Engineering fatty acid synthases for directed polyketide production.Nature chemical biology · 2017Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 Å resolution.
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