› 1yew

X-ray diffraction
2.8Å resolution

Crystal structure of particulate methane monooxygenase

Released:
DOI: 10.2210/pdb1yew/pdb
PDB entry 1yew coloured by chain, front view.
PDB entry 1yew coloured by chain, side view.
PDB entry 1yew coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane.
Lieberman RL, Rosenzweig AC
Nature 434 177-82 (2005)
PMID: 15674245

Function and Biology Details

Reaction catalysed: 
Methane + quinol + O(2) = methanol + quinone + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero octadecamer
hetero nonamer
PDBe Complex ID:
PDB-CPX-124230 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Particulate methane monooxygenase alpha subunit Chains: A, E, I
Molecule details ›
Chains: A, E, I
Length: 382 amino acids
Theoretical weight: 42.83 KDa
Source organism: Methylococcus capsulatus str. Bath
UniProt:
  • Canonical: G1UBD1 (Residues: 33-414; Coverage: 100%)
Gene names: MCA1796, MCA2853, pmoB, pmoB1, pmoB2
Sequence domains: Monooxygenase subunit B protein
Structure domains:
Particulate methane monooxygenase beta subunit Chains: B, F, J
Molecule details ›
Chains: B, F, J
Length: 247 amino acids
Theoretical weight: 28.45 KDa
Source organism: Methylococcus capsulatus str. Bath
Expression system: Escherichia coli
UniProt:
  • Canonical: Q607G3 (Residues: 1-247; Coverage: 100%)
Gene names: MCA1797, MCA2854, pmoA, pmoA1, pmoA2
Sequence domains: Ammonia monooxygenase
Structure domains: Ammonia/particulate methane monooxygenase, subunit A
Methane monooxygenase subunit C2 Chains: C, G, K
Molecule details ›
Chains: C, G, K
Length: 289 amino acids
Theoretical weight: 33.21 KDa
Source organism: Methylococcus capsulatus
Expression system: Escherichia coli
UniProt:
  • Canonical: O05111 (Residues: 1-289; Coverage: 100%)
Gene name: pmoC2
Sequence domains: Ammonia monooxygenase/methane monooxygenase, subunit C
Structure domains: Particulate methane monooxygenase subunit c2. Chain: C

Ligands and Environments

3 bound ligands:
Ligand CU 3 x CU
Ligand ZN 8 x ZN
Ligand CUA 3 x CUA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P42212
Unit cell:
a: 264.14Å b: 264.14Å c: 150.005Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.273 0.272 0.302
Expression system: Escherichia coli

Quick links

Citations

52 review citations

Metalloproteins and metal sensing.
Waldron et al. (2009)
51 more

21 mentions without citation

Enzymatic oxidation of methane.
Sirajuddin et al. (2015)
20 more