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Titolo:
Solution structure of the ribosome recycling factor from Aquifex aeolicus
Autore:
Yoshida, T; Uchiyama, S; Nakano, H; Kashimori, H; Kijima, H; Ohshima, T; Saihara, Y; Ishino, T; Shimahara, H; Yoshida, T; Yokose, K; Ohkubo, T; Kaji, A; Kobayashi, Y;
Indirizzi:
Osaka Univ, Grad Sch Pharmaceut Sci, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 eut Sci, Suita, Osaka 5650871, Japan RRF Res Inc, Tsukuba, Ibaraki 3050856, Japan RRF Res Inc Tsukuba Ibaraki Japan 3050856 Tsukuba, Ibaraki 3050856, Japan Univ Penn, Sch Med, Dept Microbiol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Microbiol, Philadelphia, PA 19104 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 8, volume: 40, anno: 2001,
pagine: 2387 - 2396
SICI:
0006-2960(20010227)40:8<2387:SSOTRR>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ROTATIONAL DIFFUSION ANISOTROPY; NUCLEAR MAGNETIC-RESONANCE; ELONGATION-FACTOR-G; RELEASE FACTOR RF3; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; FACTOR RRF; ANGSTROM-RESOLUTION; THERMUS-THERMOPHILUS; 3-DIMENSIONAL STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Kobayashi, Y Osaka Univ, Grad Sch Pharmaceut Sci, 1-6 Yamadaoka, Suita, Osaka 5650871, Japan Osaka Univ 1-6 Yamadaoka Suita Osaka Japan 5650871 871, Japan
Citazione:
T. Yoshida et al., "Solution structure of the ribosome recycling factor from Aquifex aeolicus", BIOCHEM, 40(8), 2001, pp. 2387-2396

Abstract

The solution structure of ribosome recycling factor (RRF) from hyperthermophilic bacterium, Aquifex aeolicus, was determined by heteronuclear multidimensional NMR spectroscopy. Fifteen structures were calculated using restraints derived from NOE. J-coupling, and T-1/T-2 anisotropies. The resulting structure has an overall L-shaped conformation with two domains and is similar to that of a tRNA molecule. The domain I (corresponding to the anticodon stem of tRNA) is a rigid three alpha -helix bundle. Being slightly different from usual coiled-coil arrangements, each helix of domain I is not twisted but straight and parallel to the main axis. The domain II (corresponding to the portion with the CCA end of tRNA) is an alpha/beta domain with an alpha -helix and two beta -sheets, that has some flexible regions. The backbone atomic root-mean-square deviation (rmsd) values of both domains were 0.7 Angstrom when calculated separately, which is smaller than that of the molecule as a whole (1.4 A). Measurement of N-15-{H-1} NOE values show that the residues in the corner of the L-shaped molecule are undergoing fast internal motion. These results indicate that the joint region between two domains contributes to the fluctuation in the orientation of two domains. Thus,it was shown that RRF remains the tRNA mimicry in solution where it functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 17:45:59