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Structure paper

TitleStructure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site
Journal, issue, pagesJ. Mol. Biol., Vol. 373, Page 141-152, Year 2007
Publish dateApr 27, 2007 (structure data deposition date)
AuthorsKataoka, K. / Komori, H. / Ueki, Y. / Konno, Y. / Kamitaka, Y. / Kurose, S. / Tsujimura, S. / Higuchi, Y. / Kano, K. / Seo, D. / Sakurai, T.
External linksJ. Mol. Biol. / PubMed:17804014
MethodsX-ray diffraction
Resolution1.06 - 1.81 Å
Structure data

PDB-2yxv:
The deletion mutant of Multicopper Oxidase CueO
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-2yxw:
The deletion mutant of Multicopper Oxidase CueO
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-4e9q:
Multicopper Oxidase CueO (data2)
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-4e9r:
Multicopper Oxidase CueO (data4)
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-4e9s:
Multicopper Oxidase CueO (data5)
Method: X-RAY DIFFRACTION / Resolution: 1.06 Å

PDB-4e9t:
Multicopper Oxidase CueO (data6)
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-NO3:
NITRATE ION

ChemComp-C2O:
CU-O-CU LINKAGE

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / multicopper oxidase / METAL BINDING PROTEIN

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