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Titolo:
ZINC COORDINATION IN THE DNA-BINDING DOMAIN OF THE YEAST TRANSCRIPTIONAL ACTIVATOR PPR1
Autore:
BALL LJ; DIAKUN GP; GADHAVI PL; YOUNG NA; ARMSTRONG EM; GARNER CD; LAUE ED;
Indirizzi:
DEPT BIOCHEM,TENNIS COURT RD CAMBRIDGE CB2 1QW ENGLAND DEPT BIOCHEM CAMBRIDGE CB2 1QW ENGLAND DARESBURY LAB,DRAL WARRINGTON WA4 4AD CHESHIRE ENGLAND UNIV MANCHESTER,DEPT CHEM MANCHESTER M13 9PL LANCS ENGLAND
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 358, anno: 1995,
pagine: 278 - 282
SICI:
0014-5793(1995)358:3<278:ZCITDD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; GAL4; CLUSTER;
Keywords:
PPR1; STRUCTURE; DNA BINDING DOMAIN; EXTENDED X-RAY ABSORPTION FINE STRUCTURE; EXAFS; METAL ION CLUSTER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
L.J. Ball et al., "ZINC COORDINATION IN THE DNA-BINDING DOMAIN OF THE YEAST TRANSCRIPTIONAL ACTIVATOR PPR1", FEBS letters, 358(3), 1995, pp. 278-282

Abstract

The structure of the native zinc form of the DNA binding domain in the yeast transcriptional activator PPR1 was investigated by extended X-ray absorption fine structure (EXAFS). By carrying out the EXAFS measurements at 11k we were able to demonstrate explicitly the proximity ofthe two zinc ions (Zn-Zn distance = 3.16 +/- 0.03 Angstrom) and the presence of bridging cysteine ligands. The results show that the six cysteine residues co-ordinate two zinc ions in a two-metal ion cluster. PPR1 is the first member of this class of protein for which such information has been obtained.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 12:22:02