1JK9

Heterodimer between H48F-ySOD1 and yCCS

1JK9 の概要

• エントリーDOI: 10.2210/pdb1jk9/pdb
• 分子名称: superoxide dismutase, copper chaperone for superoxide dismutase, ZINC ION, ... (5 entities in total)
• 機能のキーワード: protein-protein complex, heterodimer, metallochaperone, chaperone, copper, amyotrophic lateral sclerosis, lou gehrig's disease, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Cytoplasm: P00445 P40202
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 86682.35

構造登録者

Lamb, A.L.,Torres, A.S.,O'Halloran, T.V.,Rosenzweig, A.C. (登録日: 2001-07-11, 公開日: 2001-09-05, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)