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Titolo:
Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: Crystallographic, mutagenesis and resonance Raman spectroscopic studies
Autore:
Miyatake, H; Mukai, M; Park, SY; Adachi, S; Tamura, K; Nakamura, H; Nakamura, K; Tsuchiya, T; Iizuka, T; Shiro, Y;
Indirizzi:
RIKEN, Harima Inst, Sayo, Hyogo 6795148, Japan RIKEN Sayo Hyogo Japan 6795148 N, Harima Inst, Sayo, Hyogo 6795148, Japan Tokyo Med & Dent Univ, Dept Mol Genet, Inst Med Res, Bunkyo Ku, Tokyo 1138510, Japan Tokyo Med & Dent Univ Tokyo Japan 1138510 unkyo Ku, Tokyo 1138510, Japan
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 2, volume: 301, anno: 2000,
pagine: 415 - 431
SICI:
0022-2836(20000811)301:2<415:SMOOSF>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
KINASE-ACTIVITY; STRUCTURAL BASIS; HEME PROTEIN; DOMAIN; BINDING; AUTOXIDATION; BACTERIA; STATE; IRON;
Keywords:
crystal structure; FixL; heme protein; oxygen sensor; two-component regulatory system;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Miyatake, H RIKEN, Harima Inst, SPring 8,1-1-1 Koto Mikazuki Cho, Sayo, Hyogo 6795148,Japan RIKEN SPring 8,1-1-1 Koto Mikazuki Cho Sayo Hyogo Japan 6795148
Citazione:
H. Miyatake et al., "Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: Crystallographic, mutagenesis and resonance Raman spectroscopic studies", J MOL BIOL, 301(2), 2000, pp. 415-431

Abstract

FixL of Rhizobium meliloti (RmFixL) is a sensor histidine kinase of the two-component system, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to the O-2 levels. The crystal structure of the sensor domain of FixL (RmFixLH), which contains a heme (Fe-porphyrin) as a sensing site, was determined at 1.4 Angstrom resolution. Based on the structural and spectroscopic analyses, we propose the O-2 sensing mechanism that differs from the case proposed in BjFixLH as follows; conformational changes in the F/G loop, which are induced by steric repulsion between the bent-bound O-2 and the Ile209 side-chain, would be transmitted to the histidine kinase domain. Interaction between the iron-bound O-2, and Ile209 was also observed in the resonance Raman spectra of RmFixLH asevidenced by the fact that the Fe-O-2 and Fe-CN stretching frequencies were shifted from 575 to 570 cm(-1) (Fe-O-2), and 504 to 499 cm(-1), respectively, as the result of the replacement of Ile209 with an Ala residue. In theI209A mutant of RmFixL, the O-2 sensing activity was destroyed, thus confirming our proposed mechanism. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 20:21:00