› 3sqg

X-ray diffraction
2.1Å resolution

Crystal structure of a methyl-coenzyme M reductase purified from Black Sea mats

Released:
DOI: 10.2210/pdb3sqg/pdb
PDB entry 3sqg coloured by chain, front view.
PDB entry 3sqg coloured by chain, side view.
PDB entry 3sqg coloured by chain, top view.
Source organism: uncultured archaeon
Primary publication:
Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically.
Shima S, Krueger M, Weinert T, Demmer U, Kahnt J, Thauer RK, Ermler U
Nature 481 98-101 (2011)
PMID: 22121022

Function and Biology Details

Reaction catalysed: 
Methyl-CoM + CoB = CoM-S-S-CoB + methane
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112305 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Methyl-coenzyme M reductase subunit alpha Chains: A, D, G
Molecule details ›
Chains: A, D, G
Length: 579 amino acids
Theoretical weight: 63.86 KDa
Source organism: uncultured archaeon
UniProt:
  • Canonical: D1JBK4 (Residues: 1-579; Coverage: 100%)
Gene names: BSM_29630, mcrA
Sequence domains:
Structure domains:
coenzyme-B sulfoethylthiotransferase Chains: B, E, H
Molecule details ›
Chains: B, E, H
Length: 433 amino acids
Theoretical weight: 46.03 KDa
Source organism: uncultured archaeon
UniProt:
  • Canonical: D1JBK2 (Residues: 1-433; Coverage: 100%)
Gene names: BSM_29610, mcrB
Sequence domains:
Structure domains:
coenzyme-B sulfoethylthiotransferase Chains: C, F, I
Molecule details ›
Chains: C, F, I
Length: 279 amino acids
Theoretical weight: 31.58 KDa
Source organism: uncultured archaeon
UniProt:
  • Canonical: D1JBK3 (Residues: 1-279; Coverage: 100%)
Gene names: BSM_29620, mcrG
Sequence domains: Methyl-coenzyme M reductase gamma subunit
Structure domains: Methyl-coenzyme M reductase, gamma subunit

Ligands and Environments


Cofactor: Ligand M43 3 x M43

Cofactor: Ligand COM 3 x COM

Cofactor: Ligand TP7 3 x TP7
7 bound ligands:
Ligand 1PE 6 x 1PE
Ligand PGE 6 x PGE
Ligand SO4 9 x SO4
Ligand CL 1 x CL
Ligand CA 2 x CA
Ligand P6G 1 x P6G
Ligand GOL 2 x GOL
4 modified residues:
Ligand MHS 3 x MHS
Ligand 0AF 3 x 0AF
Ligand GL3 3 x GL3
Ligand MHO 3 x MHO

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 128.86Å b: 412.49Å c: 165.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.206

Quick links

Citations

13 review citations

Metabolic versatility in methanogens.
Costa et al. (2014)
12 more

5 mentions without citation

Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.
Lawton et al. (2016)
4 more