1JK9

Heterodimer between H48F-ySOD1 and yCCS

Summary for 1JK9

• Entry DOI: 10.2210/pdb1jk9/pdb
• Descriptor: superoxide dismutase, copper chaperone for superoxide dismutase, ZINC ION, ... (5 entities in total)
• Functional Keywords: protein-protein complex, heterodimer, metallochaperone, chaperone, copper, amyotrophic lateral sclerosis, lou gehrig's disease, oxidoreductase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm: P00445 P40202
• Total number of polymer chains: 4
• Total formula weight: 86682.35

Authors

Lamb, A.L.,Torres, A.S.,O'Halloran, T.V.,Rosenzweig, A.C. (deposition date: 2001-07-11, release date: 2001-09-05, Last modification date: 2024-11-06)

Primary citation

Lamb, A.L.,Torres, A.S.,O'Halloran, T.V.,Rosenzweig, A.C.
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone.
Nat.Struct.Biol., 8:751-755, 2001

PubMed Abstract: The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1). The 2.9 A resolution structure of yeast SOD1 complexed with yeast CCS (yCCS) reveals that SOD1 interacts with its metallochaperone to form a complex comprising one monomer of each protein. The heterodimer interface is remarkably similar to the SOD1 and yCCS homodimer interfaces. Striking conformational rearrangements are observed in both the chaperone and target enzyme upon complex formation, and the functionally essential C-terminal domain of yCCS is well positioned to play a key role in the metal ion transfer mechanism. This domain is linked to SOD1 by an intermolecular disulfide bond that may facilitate or regulate copper delivery.

PubMed: 11524675
DOI: 10.1038/nsb0901-751

Experimental method

X-RAY DIFFRACTION (2.9 Å)