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TitleThe carbon monoxide dehydrogenase accessory protein CooJ is a histidine-rich multidomain dimer containing an unexpected Ni(II)-binding site.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 7601-7614, Year 2019
Publish dateSep 5, 2018 (structure data deposition date)
AuthorsAlfano, M. / Perard, J. / Carpentier, P. / Basset, C. / Zambelli, B. / Timm, J. / Crouzy, S. / Ciurli, S. / Cavazza, C.
External linksJ. Biol. Chem. / PubMed:30858174
MethodsX-ray diffraction
Resolution2.042 Å
Structure data

PDB-6hk5:
X-ray structure of a truncated mutant of the metallochaperone CooJ with a high-affinity nickel-binding site
Method: X-RAY DIFFRACTION / Resolution: 2.042 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-CL:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-Z3P:
3,3',3''-phosphoryltripropanoic acid

ChemComp-HOH:
WATER

Source
  • rhodospirillum rubrum (bacteria)
KeywordsMETAL BINDING PROTEIN / metallochaperone / nickel-binding

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