Crystal structure of the copper chaperone for superoxide dismutase

A. L. Lamb, A. K. Wernimont, R. A. Pufahl, V. C. Culotta, T. V. O'Halloran, A. C. Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

176 Scopus citations


Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 Å resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone.

Original languageEnglish (US)
Pages (from-to)724-729
Number of pages6
JournalNature Structural Biology
Issue number8
StatePublished - 1999

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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