› 1mg2

X-ray diffraction
2.25Å resolution

MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN

Released:
DOI: 10.2210/pdb1mg2/pdb
PDB entry 1mg2 coloured by chain, front view.
PDB entry 1mg2 coloured by chain, side view.
PDB entry 1mg2 coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin.
Sun D, Chen ZW, Mathews FS, Davidson VL
Biochemistry 41 13926-33 (2002)
PMID: 12437349

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 domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-149614 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Methylamine dehydrogenase heavy chain Chains: A, E, I, M
Molecule details ›
Chains: A, E, I, M
Length: 390 amino acids
Theoretical weight: 42.67 KDa
Source organism: Paracoccus denitrificans
Expression system: Cereibacter sphaeroides
UniProt:
  • Canonical: P29894 (Residues: 28-417; Coverage: 100%)
Gene name: mauB
Sequence domains: Methylamine dehydrogenase heavy chain (MADH)
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Methylamine dehydrogenase light chain Chains: B, F, J, N
Molecule details ›
Chains: B, F, J, N
Length: 131 amino acids
Theoretical weight: 14.21 KDa
Source organism: Paracoccus denitrificans
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
Amicyanin Chains: C, G, K, O
Molecule details ›
Chains: C, G, K, O
Length: 105 amino acids
Theoretical weight: 11.51 KDa
Source organism: Paracoccus denitrificans
Expression system: Cereibacter sphaeroides
UniProt:
  • Canonical: P22364 (Residues: 27-131; Coverage: 100%)
Gene names: ami, mauC
Sequence domains: Copper binding proteins, plastocyanin/azurin family
Structure domains: Cupredoxins - blue copper proteins
Cytochrome c-L Chains: D, H, L, P
Molecule details ›
Chains: D, H, L, P
Length: 155 amino acids
Theoretical weight: 17.09 KDa
Source organism: Paracoccus denitrificans
Expression system: Cereibacter sphaeroides
UniProt:
  • Canonical: P29899 (Residues: 23-177; Coverage: 100%)
Gene name: moxG
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEC 4 x HEC
3 bound ligands:
Ligand PO4 8 x PO4
Ligand CU 4 x CU
Ligand NA 4 x NA
1 modified residue:
Ligand TRQ 4 x TRQ

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 79.122Å b: 188.201Å c: 127.1Å
α: 90° β: 99.24° γ: 90°
R-values:
R R work R free
0.173 0.173 0.21
Expression system: Cereibacter sphaeroides

Quick links

Citations

4 review citations

The Current State of NAD+ -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.
Schiedel et al. (2018)
3 more

3 mentions without citation

Variation in DNA methylation patterns of grapevine somaclones (Vitis vinifera L.).
Schellenbaum et al. (2008)
2 more