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Titolo:
STRUCTURAL COMPARISON OF CUPREDOXIN DOMAINS - DOMAIN RECYCLING TO CONSTRUCT PROTEINS WITH NOVEL FUNCTIONS
Autore:
MURPHY MEP; LINDLEY PF; ADMAN ET;
Indirizzi:
UNIV WASHINGTON,DEPT BIOL STRUCT,BOX 357420 SEATTLE WA 98195 UNIV WASHINGTON,DEPT BIOL STRUCT SEATTLE WA 98195
Titolo Testata:
Protein science
fascicolo: 4, volume: 6, anno: 1997,
pagine: 761 - 770
SICI:
0961-8368(1997)6:4<761:SCOCD->2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAY CRYSTAL-STRUCTURE; NITRITE REDUCTASE; ACHROMOBACTER-CYCLOCLASTES; ASCORBATE OXIDASE; COPPER PROTEIN; BETA-BARREL; FET3 GENE; RESOLUTION; PROGRAM; EVOLUTION;
Keywords:
CUPREDOXIN; DOMAIN PHYLOGENY; STRUCTURAL COMPARISON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M.E.P. Murphy et al., "STRUCTURAL COMPARISON OF CUPREDOXIN DOMAINS - DOMAIN RECYCLING TO CONSTRUCT PROTEINS WITH NOVEL FUNCTIONS", Protein science, 6(4), 1997, pp. 761-770

Abstract

The three-dimensional structures of the copper-containing enzymes ascorbate oxidase, ceruloplasmin, and nitrite reductase, comprised of multiple domains with a cupredoxin fold, are consistent with having evolved from a common ancestor. The presence or absence of copper sites hascomplicated ascertaining the structural and evolutionary relationshipamong these and related proteins. Simultaneous structural superposition of the enzyme domains and their known cupredoxin relatives shows clearly that there are at least six cupredoxin classes, and that the evolution of the conserved core of these domains is independent of the presence or absence of copper sites. Relationships among the variable loops in these structures show that the two-domain ancestor of the blue oxidases contained a trinuclear-copper interface but could not have functioned in a monomeric state. Comparison of the sequence of the copper-containing, iron-regulating protein. Ferrous transport (Fet3) from yeast to the structurally defined core and loop residues of the cupredoxins suggests specific residues that could be involved in the ferroxidase activity of Fet3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 04:21:19