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TitleA Histidine Residue and a Tetranuclear Cuprous-thiolate Cluster Dominate the Copper Loading Landscape of a Copper Storage Protein from Streptomyces lividans.
Journal, issue, pagesChemistry, Vol. 25, Page 10678-10688, Year 2019
Publish dateDec 7, 2018 (structure data deposition date)
AuthorsStraw, M.L. / Hough, M.A. / Wilson, M.T. / Worrall, J.A.R.
External linksChemistry / PubMed:31111982
MethodsX-ray diffraction
Resolution1.18 - 1.9 Å
Structure data

PDB-6q58:
Copper loading to a cytosolic copper storage protein from Streptomyces lividans (five coppers)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6q6b:
Structure of the copper storage protein, Ccsp, from Streptomyces lividans loaded with 10 copper equivalents
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6qvh:
Streptomyces lividans Ccsp mutant - H113A
Method: X-RAY DIFFRACTION / Resolution: 1.28 Å

PDB-6qyb:
Streptomyces lividans Ccsp mutant - H111A
Method: X-RAY DIFFRACTION / Resolution: 1.18 Å

PDB-6r01:
Streptomyces lividans Ccsp mutant - H107A/H111A
Method: X-RAY DIFFRACTION / Resolution: 1.18 Å

Chemicals

ChemComp-CU1:
COPPER (I) ION

ChemComp-HOH:
WATER

ChemComp-CU:
COPPER (II) ION

Source
  • streptomyces coelicolor 1326 (bacteria)
  • streptomyces lividans 1326 (bacteria)
KeywordsMETAL BINDING PROTEIN / Copper / cytosolic / storage protein / Streptomyces livdians / storage / Streptomyces lividans / homeostasis / toxicity / Streptomyces

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