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

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 71; no. 11; pp. 1401 - 1407
• Main Authors: Enderle, Mathias, McCarthy, Andrew, Paithankar, Karthik Shivaji, Grininger, Martin
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.11.2015; Wiley Subscription Services, Inc
• 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; fatty-acid synthase; mycolic acid; fatty-acid synthesis; multienzyme; tuberculosis
• ISSN: 2053-230X; 2053-230X
• DOI: 10.1107/S2053230X15018336

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.