6GJC

Structure of Mycobacterium tuberculosis Fatty Acid Synthase - I

This is a non-PDB format compatible entry.

Summary for 6GJC

• Entry DOI: 10.2210/pdb6gjc/pdb
• EMDB information: 0011
• Descriptor: Fatty acid synthase, FLAVIN MONONUCLEOTIDE (2 entities in total)
• Functional Keywords: fatty acid synthesis, tuberculosis, biosynthetic protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 6
• Total formula weight: 1978878.56

Authors

Elad, N.,Baron, S.,Shakked, Z.,Zimhony, O.,Diskin, R. (deposition date: 2018-05-16, release date: 2018-09-05, Last modification date: 2024-05-15)

Primary citation

Elad, N.,Baron, S.,Peleg, Y.,Albeck, S.,Grunwald, J.,Raviv, G.,Shakked, Z.,Zimhony, O.,Diskin, R.
Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 angstrom resolution.
Nat Commun, 9:3886-3886, 2018

PubMed Abstract: Tuberculosis (TB) is a devastating and rapidly spreading disease caused by Mycobacterium tuberculosis (Mtb). Therapy requires prolonged treatment with a combination of multiple agents and interruptions in the treatment regimen result in emergence and spread of multi-drug resistant (MDR) Mtb strains. MDR Mtb poses a significant global health problem, calling for urgent development of novel drugs to combat TB. Here, we report the 3.3 Å resolution structure of the ~2 MDa type-I fatty acid synthase (FAS-I) from Mtb, determined by single particle cryo-EM. Mtb FAS-I is an essential enzymatic complex that contributes to the virulence of Mtb, and thus a prime target for anti-TB drugs. The structural information for Mtb FAS-I we have obtained enables computer-based drug discovery approaches, and the resolution achieved by cryo-EM is sufficient for elucidating inhibition mechanisms by putative small molecular weight inhibitors.

PubMed: 30250274
DOI: 10.1038/s41467-018-06440-6

Experimental method

ELECTRON MICROSCOPY (3.3 Å)