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Titolo:
RIBONUCLEASE-P PROTEIN-STRUCTURE - EVOLUTIONARY ORIGINS IN THE TRANSLATIONAL APPARATUS
Autore:
STAMS T; NIRANJANAKUMARI S; FIERKE CA; CHRISTIANSON DW;
Indirizzi:
UNIV PENN,DEPT CHEM,ROY & DIANA VAGELOS LABS PHILADELPHIA PA 19104 UNIV PENN,DEPT CHEM,ROY & DIANA VAGELOS LABS PHILADELPHIA PA 19104 DUKE UNIV,MED CTR,DEPT BIOCHEM DURHAM NC 27710
Titolo Testata:
Science
fascicolo: 5364, volume: 280, anno: 1998,
pagine: 752 - 755
SICI:
0036-8075(1998)280:5364<752:RP-EOI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
GEL RETARDATION ANALYSIS; ELONGATION-FACTOR-G; COLI RNASE-P; 4.5 S-RNA; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; M1 RNA; MAGNESIUM-IONS; CATALYTIC RNA; NUCLEOTIDE-SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
T. Stams et al., "RIBONUCLEASE-P PROTEIN-STRUCTURE - EVOLUTIONARY ORIGINS IN THE TRANSLATIONAL APPARATUS", Science, 280(5364), 1998, pp. 752-755

Abstract

The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalyticactivity. Mutagenesis and biochemical data indicate that an unusual left-handed beta alpha beta crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.

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Documento generato il 05/04/20 alle ore 09:32:30