› 5zzw

X-ray diffraction
2.6Å resolution

Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA

Released:
DOI: 10.2210/pdb5zzw/pdb
PDB entry 5zzw coloured by chain, front view.
PDB entry 5zzw coloured by chain, side view.
PDB entry 5zzw coloured by chain, top view.
Source organism: Dictyostelium discoideum
Primary publication:
Proteobacterial Origin of Protein Arginine Methylation and Regulation of Complex I Assembly by MidA.
Shahul Hameed UF, Sanislav O, Lay ST, Annesley SJ, Jobichen C, Fisher PR, Swaminathan K, Arold ST
Cell Rep 24 1996-2004 (2018)
PMID: 30134162

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-arginine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine methyltransferase NDUFAF7 homolog, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 414 amino acids
Theoretical weight: 46.93 KDa
Source organism: Dictyostelium discoideum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54S83 (Residues: 76-484; Coverage: 85%)
Gene names: DDB_G0282615, midA
Sequence domains: Putative S-adenosyl-L-methionine-dependent methyltransferase

Ligands and Environments

1 bound ligand:
Ligand SAH 3 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P212121
Unit cell:
a: 72.95Å b: 103.54Å c: 192.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.248 0.28
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The Biological Axis of Protein Arginine Methylation and Asymmetric Dimethylarginine.
Fulton et al. (2019)
2 more