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

Enderle, Mathias; McCarthy, Andrew; Paithankar, Karthik Shivaji; Grininger, Martin

doi:10.1107/S2053230X15018336

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

/persons/resource/persons77936

Enderle, Mathias
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78032

Grininger, Martin
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

no5090.pdf
(Any fulltext), 737KB

Supplementary Material (public)

There is no public supplementary material available

Citation

Enderle, M., McCarthy, A., Paithankar, K. S., & Grininger, M. (2015). Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 71, 1401-1407. doi:10.1107/S2053230X15018336.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-3A4E-F

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 angstrom resolution.