1QUP

CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE

Summary for 1QUP

• Entry DOI: 10.2210/pdb1qup/pdb
• Descriptor: SUPEROXIDE DISMUTASE 1 COPPER CHAPERONE, SULFATE ION (3 entities in total)
• Functional Keywords: two domains, beta-alpha-beta-beta-alpha-beta and beta barrel, chaperone
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 48998.40

Authors

Lamb, A.L.,Wernimont, A.K.,Pufahl, R.A.,O'Halloran, T.V.,Rosenzweig, A.C. (deposition date: 1999-07-01, release date: 1999-12-10, Last modification date: 2024-10-09)

Primary citation

Lamb, A.L.,Wernimont, A.K.,Pufahl, R.A.,Culotta, V.C.,O'Halloran, T.V.,Rosenzweig, A.C.
Crystal structure of the copper chaperone for superoxide dismutase.
Nat.Struct.Biol., 6:724-729, 1999

PubMed 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.

PubMed: 10426947
DOI: 10.1038/11489

Experimental method

X-RAY DIFFRACTION (1.8 Å)