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Titolo:
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
Autore:
Lamb, AL; Torres, AS; OHalloran, TV; Rosenzweig, AC;
Indirizzi:
Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ Evanston IL USA 60208 Cell Biol, Evanston, IL 60208 USA Northwestern Univ, Dept Chem, Evanston, IL 60208 USA Northwestern Univ Evanston IL USA 60208 Dept Chem, Evanston, IL 60208 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 9, volume: 8, anno: 2001,
pagine: 751 - 755
SICI:
1072-8368(200109)8:9<751:HSOSDI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYOTROPHIC-LATERAL-SCLEROSIS; HUMAN COPPER CHAPERONE; CRYSTAL-STRUCTURE; SACCHAROMYCES-CEREVISIAE; ELECTRON-DENSITY; PROTEIN; YEAST; METAL; TRANSPORT; CLUSTER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Rosenzweig, AC Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ Evanston IL USA 60208 ston, IL 60208 USA
Citazione:
A.L. Lamb et al., "Heterodimeric structure of superoxide dismutase in complex with its metallochaperone", NAT ST BIOL, 8(9), 2001, pp. 751-755

Abstract

The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1). The 2.9 Angstrom resolution structure of yeast SOD1 complexed with yeast CCS (yCCS) reveals that SOD I interacts with its metallochaperone to form a complex comprising one monomer of each protein. The heterodimer interface is remarkablysimilar to the SOD1 and yCCS homodimer interfaces. Striking conformationalrearrangements 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 SOD I by an intermolecular disulfide bond that mayfacilitate or regulate copper delivery.

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Documento generato il 05/04/20 alle ore 06:58:15