6GJC

Structure of Mycobacterium tuberculosis Fatty Acid Synthase - I


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 angstrom resolution.

Elad, N.Baron, S.Peleg, Y.Albeck, S.Grunwald, J.Raviv, G.Shakked, Z.Zimhony, O.Diskin, R.

(2018) Nat Commun 9: 3886-3886

  • DOI: https://doi.org/10.1038/s41467-018-06440-6
  • Primary Citation of Related Structures:  
    6GJC

  • 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.


  • Organizational Affiliation

    Department of Chemical Research Support, Weizmann Institute of Science, Rehovot, 7610001, Israel.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fatty acid synthase
A, B, C, D, E
A, B, C, D, E, F
3,092Mycobacterium tuberculosisMutation(s): 0 
Gene Names: kasA_1kasA_2C0088_13835ERS124361_00292SAMEA2682864_02566
EC: 2.3.1.41
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION
MODEL REFINEMENTPHENIX

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-09-05
    Type: Initial release
  • Version 1.1: 2018-10-10
    Changes: Data collection, Database references
  • Version 1.2: 2019-12-11
    Changes: Other