Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C.
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.
Tanaka
Tomoyuki
T
RIKEN SPring-8 Center, Harima Institute, Kouto, Sayo, Hyogo 679-5148, Japan.
Sawano
Masahide
M
Ogasahara
Kyoko
K
Sakaguchi
Yasushi
Y
Bagautdinov
Bagautdin
B
Katoh
Etsuko
E
Kuroishi
Chizu
C
Shinkai
Akeo
A
Yokoyama
Shigeyuki
S
Yutani
Katsuhide
K
D019843:Archaeal Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006358:Hot Temperature; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D043902:Pyrococcus horikoshii / Q000737:chemistry*; D040681:Structural Homology, Protein; D016963:Thermus thermophilus / Q000737:chemistry*
D019843:Archaeal Proteins; C094846:CutA protein, E coli; D029968:Escherichia coli Proteins