| Literature DB >> 2263451 |
M E Peter1, C O Reiser, N K Schirmer, T Kiefhaber, G Ott, N W Grillenbeck, M Sprinzl.
Abstract
The middle and C-terminal domain (domain II/III) of elongation factor Tu from Thermus thermophilus lacking the GTP/GDP binding domain have been prepared by treating nucleotide-free protein with Staphylococcus aureus V8 protease. The isolated domain II/III of EF-Tu has a compact structure and high resistance against tryptic treatment and thermal denaturation. As demonstrated by circular dichroism spectroscopy, the isolated domain II/III does not contain any alpha-helical structure. Nucleotide exchange factor, EF-Ts, was found to interact with domain II/III, whereas the binding of aminoacyl-tRNA, GDP and GTP to this EF-Tu fragment could not be detected.Entities:
Mesh:
Substances:
Year: 1990 PMID: 2263451 PMCID: PMC332746 DOI: 10.1093/nar/18.23.6889
Source DB: PubMed Journal: Nucleic Acids Res ISSN: 0305-1048 Impact factor: 16.971