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Titolo:
Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus
Autore:
Leonard, PM; Smits, SHJ; Sedelnikova, SE; Brinkman, AB; de Vos, WM; van der Oost, J; Rice, DW; Rafferty, JB;
Indirizzi:
Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Sheffield S Yorkshire England S10 2TN S Yorkshire, England Agr Univ Wageningen, Microbiol Lab, NL-6703 CT Wageningen, Netherlands AgrUniv Wageningen Wageningen Netherlands NL-6703 CT ingen, Netherlands
Titolo Testata:
EMBO JOURNAL
fascicolo: 5, volume: 20, anno: 2001,
pagine: 990 - 997
SICI:
0261-4189(20010301)20:5<990:CSOTLT>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI LRP; MACROMOLECULAR STRUCTURES; GLOBAL REGULATOR; BINDING DOMAIN; DNA-POLYMERASE; B-DNA; PROTEIN; LEUCINE; GENE; IDENTIFICATION;
Keywords:
helix-turn-helix; Lrp-AsnC family; Pyrococcus furiosus; transcriptional regulator; X-ray crystallography;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Rafferty, JB Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Sheffield SYorkshire England S10 2TN England
Citazione:
P.M. Leonard et al., "Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus", EMBO J, 20(5), 2001, pp. 990-997

Abstract

The LrpA protein from the hyperthermophilic archaeon Pyrococcusfuriosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 Angstrom resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpAforms a homodimer mainly through interactions between the antiparallel beta -sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled tomutational analysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 22:03:24