| Literature DB >> 16831434 |
Tomoyuki Tanaka1, Masahide Sawano, Kyoko Ogasahara, Yasushi Sakaguchi, Bagautdin Bagautdinov, Etsuko Katoh, Chizu Kuroishi, Akeo Shinkai, Shigeyuki Yokoyama, Katsuhide Yutani.
Abstract
We found that the CutA1 protein, from Pyrococcus horikoshii (PhCutA1), has an extremely high denaturation temperature (T(d)) of nearly 150 degrees C, which exceeds the highest record determined by DSC by about 30 degrees C. To elucidate the mechanism of the ultra-high stability of PhCutA1, we analyzed the crystal structures of CutA1 proteins from three different sources, P. horikoshii, Thermus thermophilus, and Escherichia coli, with different growth temperatures (98, 75, and 37 degrees C). This analysis revealed that the remarkably increased number of ion pairs in the monomeric structure contributes to the stabilization of the trimeric structure and plays an important role in enhancing the T(d), up to 150 degrees C, for PhCutA1.Entities:
Mesh：
Substances：
Year: 2006 PMID： 16831434 DOI： 10.1016/j.febslet.2006.06.084
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124