› 2vow

X-ray diffraction
1.65Å resolution

An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of recombinant MopE to 1.65AA

Released:
DOI: 10.2210/pdb2vow/pdb
PDB entry 2vow coloured by chain, front view.
PDB entry 2vow coloured by chain, side view.
PDB entry 2vow coloured by chain, top view.
Source organism: Methylococcus capsulatus str. Bath
Primary publication:
An oxidized tryptophan facilitates copper binding in Methylococcus capsulatus-secreted protein MopE.
Helland R, Fjellbirkeland A, Karlsen OA, Ve T, Lillehaug JR, Jensen HB
J Biol Chem 283 13897-904 (2008)
PMID: 18348978

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper(I)-binding protein CorA domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 336 amino acids
Theoretical weight: 36.18 KDa
Source organism: Methylococcus capsulatus str. Bath
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G1UBC6 (Residues: 205-540; Coverage: 62%)
Gene names: MCA2589, mopE
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 65.28Å b: 100.67Å c: 54.65Å
α: 90° β: 97.56° γ: 90°
R-values:
R R work R free
0.183 0.181 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Methanotrophs and copper.
Semrau et al. (2010)
8 more

1 mention without citation

Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.
Gendoo et al. (2011)