› 3sle

X-ray diffraction
2.52Å resolution

Crystal Structure of the P107C-MauG/pre-Methylamine Dehydrogenase Complex

Released:
DOI: 10.2210/pdb3sle/pdb
PDB entry 3sle coloured by chain, front view.
PDB entry 3sle coloured by chain, side view.
PDB entry 3sle coloured by chain, top view.
Source organism: Paracoccus denitrificans PD1222
Primary publication:
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.
Feng M, Jensen LM, Yukl ET, Wei X, Liu A, Wilmot CM, Davidson VL
Biochemistry 51 1598-606 (2012)
PMID: 22299652

Function and Biology Details

Reaction catalysed: 
Methylamine + H(2)O + 2 oxidized [amicyanin] = formaldehyde + NH(3) + 2 reduced [amicyanin]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-106575 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Methylamine utilization protein MauG Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 41.18 KDa
Source organism: Paracoccus denitrificans PD1222
Expression system: Paracoccus denitrificans PD1222
UniProt:
  • Canonical: Q51658 (Residues: 21-387; Coverage: 100%)
Gene names: Pden_4736, mauG
Sequence domains: Di-haem cytochrome c peroxidase
Structure domains: Cytochrome c-like domain
Methylamine dehydrogenase light chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 137 amino acids
Theoretical weight: 15.03 KDa
Source organism: Paracoccus denitrificans PD1222
Expression system: Cereibacter sphaeroides
UniProt:
  • Canonical: P22619 (Residues: 58-188; Coverage: 100%)
Gene name: mauA
Sequence domains: Methylamine dehydrogenase, L chain
Structure domains: Methylamine/Aralkylamine dehydrogenase light chain
Methylamine dehydrogenase heavy chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 385 amino acids
Theoretical weight: 42.32 KDa
Source organism: Paracoccus denitrificans PD1222
Expression system: Cereibacter sphaeroides
UniProt:
  • Canonical: A1BB97 (Residues: 33-417; Coverage: 99%)
Gene name: Pden_4730
Sequence domains: Methylamine dehydrogenase heavy chain (MADH)
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase

Ligands and Environments


Cofactor: Ligand HEC 4 x HEC
3 bound ligands:
Ligand CA 2 x CA
Ligand ACT 4 x ACT
Ligand EDO 2 x EDO
2 modified residues:
Ligand CSD 2 x CSD
Ligand 0AF 2 x 0AF

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 55.851Å b: 88.53Å c: 107.698Å
α: 116.21° β: 91.83° γ: 99.35°
R-values:
R R work R free
0.178 0.174 0.243
Expression systems:
  • Paracoccus denitrificans PD1222
  • Cereibacter sphaeroides

Quick links

Citations

5 review citations

Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.
Davidson et al. (2013)
4 more

1 mention without citation

Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.
Feng et al. (2012)