+Open data
-Basic information
Entry | Database: PDB / ID: 6gjc | ||||||
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Title | Structure of Mycobacterium tuberculosis Fatty Acid Synthase - I | ||||||
Components | Fatty acid synthase | ||||||
Keywords | BIOSYNTHETIC PROTEIN / Fatty Acid Synthesis / Tuberculosis | ||||||
Function / homology | Function and homology information fatty acid synthase complex / beta-ketoacyl-[acyl-carrier-protein] synthase I / enoyl-[acyl-carrier-protein] reductase (NADH) activity / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / hydrolase activity Similarity search - Function | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||
Authors | Elad, N. / Baron, S. / Shakked, Z. / Zimhony, O. / Diskin, R. | ||||||
Citation | Journal: Nat Commun / Year: 2018 Title: Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution. Authors: Nadav Elad / Szilvia Baron / Yoav Peleg / Shira Albeck / Jacob Grunwald / Gal Raviv / Zippora Shakked / Oren Zimhony / Ron Diskin / 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 ...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. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6gjc.cif.gz | 2.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6gjc.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6gjc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6gjc_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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Full document | 6gjc_full_validation.pdf.gz | 1.9 MB | Display | |
Data in XML | 6gjc_validation.xml.gz | 395.8 KB | Display | |
Data in CIF | 6gjc_validation.cif.gz | 611.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gj/6gjc ftp://data.pdbj.org/pub/pdb/validation_reports/gj/6gjc | HTTPS FTP |
-Related structure data
Related structure data | 0011MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 329356.750 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) Gene: kasA_1, kasA_2, C0088_13835, ERS124361_00292, SAMEA2682864_02566 Production host: Escherichia coli (E. coli) References: UniProt: A0A0T9Z6H1, UniProt: A0A655MK98*PLUS, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: Chemical | ChemComp-FMN / |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Fatty Acid Synthase - I / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: Mycobacterium tuberculosis (bacteria) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7.2 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 4.49 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||
Symmetry | Point symmetry: D3 (2x3 fold dihedral) | |||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 40160 / Symmetry type: POINT | |||||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT |