Crystal structure of the copper chaperone for superoxide dismutase

Nat Struct Biol. 1999 Aug;6(8):724-9. doi: 10.1038/11489.

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 A 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins*
  • Copper / chemistry*
  • Crystallography, X-Ray
  • Fungal Proteins / chemistry
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Sequence Data
  • Protein Conformation
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid
  • Superoxide Dismutase / chemistry*

Substances

  • ATX1 protein, S cerevisiae
  • Carrier Proteins
  • Fungal Proteins
  • Molecular Chaperones
  • Saccharomyces cerevisiae Proteins
  • Copper
  • Superoxide Dismutase

Associated data

  • PDB/1QUP