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Crystallization and X‐ray diffraction studies of a complete bacterial fatty‐acid synthase type I
Author(s) -
Enderle Mathias,
McCarthy Andrew,
Paithankar Karthik Shivaji,
Grininger Martin
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15018336
Subject(s) - nocardia , fatty acid synthase , mycobacterium tuberculosis , microbiology and biotechnology , tuberculosis , biology , enzyme , corynebacterium , bacteria , fatty acid , chemistry , biochemistry , medicine , genetics , pathology
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.