TY  - JOUR
A1  - Enderle, Mathias
A1  - McCarthy, Andrew
A1  - Paithankar, Karthik Shivaji
A1  - Grininger, Martin
T1  - Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
T2  - Acta crystallographica / Section F, Structural biology communications
N2  - 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.
KW  - fatty-acid synthase
KW  - fatty-acid synthesis
KW  - multienzyme
KW  - tuberculosis
KW  - mycolic acid
Y1  - 2015
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/38687
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-386875
SN  - 2053-230X
VL  - 71
IS  - Pt 11
SP  - 1401
EP  - 1407
PB  - Blackwell
CY  - Oxford [u.a.]
ER  -