Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies
Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies
复制标题
大肠杆菌和嗜热栖热菌释放因子 2:结构、光谱和微量热研究
作者:
Gabriel Zoldá;L. Redecke;D. Svergun;P. Konarev;Stefan Voertler;H. Dobbek;Erik Sedlá;M. Sprinzl
Prokaryotic class I release factors (RFs) respond to mRNA stop codons and terminate protein synthesis. They interact with the ribosomal decoding site and the peptidyl-transferase centre bridging these 75 Å distant ribosomal centres. For this an elongated RF conformation, with partially unfolded core domains II·III·IV is required, which contrasts the known compact RF crystal structures. The crystal structure of Thermus thermophilus RF2 was determined and compared with solution structure of T. thermophilus and Escherichia coli RF2 by microcalorimetry, circular dichroism spectroscopy and small angle X-ray scattering. The structure of T. thermophilus RF2 in solution at 20°C is predominantly compact like the crystal structure. Thermodynamic analysis point to an initial melting of domain I, which is independent from the melting of the core. The core domains II·III·IV melt cooperatively at the respective physiological temperatures for T. thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome.
影响因子:
--
作者:
Ernesto Freire
通讯作者:
Ernesto Freire
影响因子:
2.9
作者:
MANAVALAN, P;JOHNSON, WC
通讯作者:
JOHNSON, WC
DOI:
10.1093/protein/13.3.179
发表时间:
2000-03-01
期刊:
PROTEIN ENGINEERING
影响因子:
--
作者:
Kumar, S;Tsai, CJ;Nussinov, R
通讯作者:
Nussinov, R