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Titolo:
Effects of charged amino-acid mutation on the solution structure of cytochrome b(5) and binding between cytochrome b(5) and cytochrome c
Autore:
Qian, CM; Yao, Y; Ye, KQ; Wang, JF; Tang, WX; Wang, YH; Wang, WH; Lu, JX; Xie, Y; Huang, ZX;
Indirizzi:
Nanjing Univ, State Key Lab Coordinat Chem, Nanjing 210093, Peoples R China Nanjing Univ Nanjing Peoples R China 210093 jing 210093, Peoples R China Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China Fudan Univ Shanghai Peoples R China 200433 nghai 200433, Peoples R China Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples RChina Acad Sinica Beijing Peoples R China 100101 eijing 100101, Peoples RChina
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 12, volume: 10, anno: 2001,
pagine: 2451 - 2459
SICI:
0961-8368(200112)10:12<2451:EOCAMO>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
NMR STRUCTURE CALCULATION; ELECTRON-TRANSFER; PARAMAGNETIC METALLOPROTEINS; PSEUDOCONTACT SHIFTS; MOLECULAR-DYNAMICS; PROTEIN STRUCTURES; COMPLEX; PROGRAM; RESOLUTION; KINETICS;
Keywords:
cytochrome b5; cytochrome c; mutant; NMR; solution structure; electrostatic interaction; binding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Tang, WX Nanjing Univ, State Key Lab Coordinat Chem, Nanjing 210093, Peoples R China Nanjing Univ Nanjing Peoples R China 210093 93, Peoples R China
Citazione:
C.M. Qian et al., "Effects of charged amino-acid mutation on the solution structure of cytochrome b(5) and binding between cytochrome b(5) and cytochrome c", PROTEIN SCI, 10(12), 2001, pp. 2451-2459

Abstract

The solution structure of oxidized bovine microsomal cytochrome b(5) mutant (E48, E56/A, D60/A) has been determined through 1524 meaningful nuclear Overhauser effect constraints together with 190 pseudocontact shift constraints. The final family of 35 conformers has rmsd values with respect to the mean structure of 0.045 +/-0.009 nm and 0.088 +/-0.011 nm for backbone and heavy atoms, respectively. A characteristic of this mutant is that of having no significant changes in the whole folding and secondary structure compared with the X-ray and solution structures of wild-type cytochrome b(5). The binding of different surface mutants of cytochrome b(5) with cytochrome cshows that electrostatic interactions play an important role in maintaining the stability and specificity of the protein complex formed. The differences in association constants demonstrate the electrostatic contributions ofcytochrome b(5), surface negatively charged residues, which were suggestedto be involved in complex formation in the Northrup and Salemme models, have cumulative effect on the stability of cyt c-cyt b(5) complex, and the contribution of Glu48 is a little higher than that of Glu44. Moreover, our result suggests that the docking geometry proposed by Northrup, which is involved in the participation of Glu48, Glu56, Asp60, and heme propionate of cytochrome b(5), do occur in the association between cytochrome b(5) and cytochrome c.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:11:07