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Titolo:
DNA lesion bypass polymerases open up
Autore:
Beard, WA; Wilson, SH;
Indirizzi:
NIEHS, Struct Biol Lab, NIH, Res Triangle Pk, NC 27709 USA NIEHS Res Triangle Pk NC USA 27709 ab, NIH, Res Triangle Pk, NC 27709 USA
Titolo Testata:
STRUCTURE
fascicolo: 9, volume: 9, anno: 2001,
pagine: 759 - 764
SICI:
0969-2126(200109)9:9<759:DLBPOU>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYMINE-THYMINE DIMER; CRYSTAL-STRUCTURES; ESCHERICHIA-COLI; NUCLEOTIDE INCORPORATION; GENE ENCODES; XERODERMA-PIGMENTOSUM; LARGE FRAGMENT; BETA; FIDELITY; ETA;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Wilson, SH NIEHS, Struct Biol Lab, NIH, POB 12233, Res Triangle Pk, NC 27709 USA NIEHS POB 12233 Res Triangle Pk NC USA 27709 e Pk, NC 27709 USA
Citazione:
W.A. Beard e S.H. Wilson, "DNA lesion bypass polymerases open up", STRUCTURE, 9(9), 2001, pp. 759-764

Abstract

Structures of catalytic fragments of two DNA lesion bypass DNA polymerases, yeast DNA polymerase eta and an archeon DinB homolog, have recently been solved. These structures share several common architectural and structural features observed in other DNA polymerases, including a hand-like architecture with fingers, palm, and thumb subdomains. The new structures provide the first structural insights into DNA lesion bypass. The fingers and thumb are smaller than those in other DNA polymerases. Modeled substrates suggest that the fingers in the vicinity of the incoming nucleotide is closed, a conformation not previously observed for an unliganded polymerase. However, the template binding pocket appears to be more open, indicating that for DNApolymerase eta, a covalently linked thymine-thymine dinner could be accommodated.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 19:33:34