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 understo...

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Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2015-11, Vol.71 (11), p.1401-1407
Main Authors: Enderle, Mathias, McCarthy, Andrew, Paithankar, Karthik Shivaji, Grininger, Martin
Format: Article
Language:English
Subjects:
Actinomycetales
Bacteria
Biology
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
Corynebacterium
Corynebacterium - enzymology
CRYSTALLIZATION
DATA ANALYSIS
Diffraction
Drugs
Fatty Acid Synthase, Type I - chemistry
Fatty Acid Synthase, Type I - isolation & purification
fatty-acid synthase
fatty-acid synthesis
Fungi
Homology
multienzyme
Mycobacterium
Mycobacterium tuberculosis - enzymology
mycolic acid
Nocardia
Research Communications
Tuberculosis
X RADIATION
X-RAY DIFFRACTION
X-rays
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description 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_str_mv 10.1107/S2053230X15018336
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2053-230X
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source Wiley-Blackwell Read & Publish Collection; PubMed Central; Free Full-Text Journals in Chemistry
subjects Actinomycetales
Bacteria
Biology
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
Corynebacterium
Corynebacterium - enzymology
CRYSTALLIZATION
DATA ANALYSIS
Diffraction
Drugs
Fatty Acid Synthase, Type I - chemistry
Fatty Acid Synthase, Type I - isolation & purification
fatty-acid synthase
fatty-acid synthesis
Fungi
Homology
multienzyme
Mycobacterium
Mycobacterium tuberculosis - enzymology
mycolic acid
Nocardia
Research Communications
Tuberculosis
X RADIATION
X-RAY DIFFRACTION
X-rays
title Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
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