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Structure paper

TitleCrystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 37849-37857, Year 2011
Publish dateJul 1, 2010 (structure data deposition date)
AuthorsSingh, S.K. / Roberts, S.A. / McDevitt, S.F. / Weichsel, A. / Wildner, G.F. / Grass, G.B. / Rensing, C. / Montfort, W.R.
External linksJ. Biol. Chem. / PubMed:21903583
MethodsX-ray diffraction
Resolution1.1 - 2.1 Å
Structure data

PDB-3nsc:
C500S MUTANT OF CueO BOUND TO Cu(II)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-3nsd:
Silver bound to the multicopper oxidase CueO (untagged)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3nsf:
Apo form of the multicopper oxidase CueO
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3nsy:
The multi-copper oxidase CueO with six Met to Ser mutations (M358S,M361S,M362S,M364S,M366S,M368S)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3nt0:
C500S (T1D) Mutant of CueO soaked in and bound to Cu(I)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3od3:
CueO at 1.1 A resolution including residues in previously disordered region
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-SO4:
SULFATE ION

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-AG:
SILVER ION

ChemComp-O:
OXYGEN ATOM

ChemComp-C2O:
CU-O-CU LINKAGE

ChemComp-CU1:
COPPER (I) ION

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / multicopper oxidase / T1 depleted C500S mutation / silver / apo form / no copper / multicopper oxidas / copper(I) / C500S mutant / cu(I) oxidase

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