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Structure paper

TitleAn Oxidized Tryptophan Facilitates Copper Binding in Methylococcus Capsulatus-Secreted Protein Mope.
Journal, issue, pagesJ. Biol. Chem., Vol. 283, Page 13897-, Year 2008
Publish dateFeb 22, 2008 (structure data deposition date)
AuthorsHelland, R. / Fjellbirkeland, A. / Karlsen, O.A. / Ve, T. / Lillehaug, J.R. / Jensen, H.B.
External linksJ. Biol. Chem. / PubMed:18348978
MethodsX-ray diffraction
Resolution1.35 - 1.9 Å
Structure data

PDB-2vov:
An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-2vow:
An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of recombinant MopE to 1.65AA
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-2vox:
An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of mercury soaked MopE to 1.9AA
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-CU:
COPPER (II) ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-HG:
Unknown entry

Source
  • methylococcus capsulatus (bacteria)
KeywordsMETAL BINDING PROTEIN / METAL-BINDING PROTEIN / OXIDIZED TRYPTOPHAN / METHANOTROPH BACTERIUM / KUNURENINE / COPPER HOMEOSTASIS

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