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

167 Scopus citations

Abstract

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
Volume6
Issue number8
DOIs
StatePublished - 1999

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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