6ADQ image
Deposition Date 2018-08-01
Release Date 2018-11-14
Last Version Date 2025-09-17
Entry Detail
PDB ID:
6ADQ
Title:
Respiratory Complex CIII2CIV2SOD2 from Mycobacterium smegmatis
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
3.50 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Rieske iron-sulfur protein Qc
Gene (Uniprot):qcrA
Chain IDs:L (auth: A), X (auth: M)
Chain Length:421
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Ubiquinol-cytochrome c reduct
Gene (Uniprot):MSMEG_4263
Chain IDs:J (auth: B), V (auth: N)
Chain Length:546
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Cytochrome bc1 complex cytoch
Gene (Uniprot):qcrC
Chain IDs:K (auth: C), W (auth: O)
Chain Length:294
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Prokaryotic respiratory super
Chain IDs:G (auth: D), S (auth: P)
Chain Length:100
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Cytochrome c oxidase subunit
Gene (Uniprot):MSMEG_4268
Chain IDs:A (auth: E), M (auth: Q)
Chain Length:341
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Cytochrome c oxidase subunit
Chain IDs:B (auth: F), N (auth: R)
Chain Length:575
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Cytochrome c oxidase subunit
Gene (Uniprot):MSMEG_4260
Chain IDs:C (auth: G), O (auth: S)
Chain Length:203
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Cytochrome c oxidase polypept
Gene (Uniprot):MSMEG_4267
Chain IDs:D (auth: H), P (auth: T)
Chain Length:139
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Cytochrome c oxidase subunit
Gene (Uniprot):MSMEG_4693
Chain IDs:E (auth: I), Q (auth: U)
Chain Length:79
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Uncharacterized protein MSMEG
Gene (Uniprot):MSMEG_4692, MSMEI_4575
Chain IDs:F (auth: J), R (auth: V)
Chain Length:157
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:LpqE protein
Gene (Uniprot):MSMEG_6078
Chain IDs:I (auth: K), U (auth: W)
Chain Length:186
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Superoxide dismutase [Cu-Zn]
Gene (Uniprot):sodC
Chain IDs:H (auth: Y), T (auth: Z)
Chain Length:236
Number of Molecules:2
Biological Source:Mycobacterium smegmatis MC2 51
Primary Citation
An electron transfer path connects subunits of a mycobacterial respiratory supercomplex.
Science 362 ? ? (2018)
PMID: 30361386 DOI: 10.1126/science.aat8923

Abstact

We report a 3.5-angstrom-resolution cryo-electron microscopy structure of a respiratory supercomplex isolated from Mycobacterium smegmatis. It comprises a complex III dimer flanked on either side by individual complex IV subunits. Complex III and IV associate so that electrons can be transferred from quinol in complex III to the oxygen reduction center in complex IV by way of a bridging cytochrome subunit. We observed a superoxide dismutase-like subunit at the periplasmic face, which may be responsible for detoxification of superoxide formed by complex III. The structure reveals features of an established drug target and provides a foundation for the development of treatments for human tuberculosis.

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