Molecular dynamics study of a hyperthermophilic
and a mesophilic rubredoxin
Grottesi A, Ceruso MA, Colosimo A,
Di Nola A
PROTEINS-STRUCTURE FUNCTION AND GENETICS
46
(3): 287-294 FEB 15 2002
Abstract:
In recent years, increased interest in the origin of protein thermal stability has gained attention both for its possible role in understanding the forces governing the folding of a protein and for the design of new highly stable engineered biocatalysts. To study the origin of thermostability, we have performed molecular dynamics simulations of two rubredoxins, from the mesophile Clostridium pasteurianum and from the hyperthermophile Pyrococcus furiosus. The simulations were carried out at two temperatures, 300 and 373 K, for each molecule. The length of the simulations was within the range of 6-7.2 ns. The rubredoxin from the hyperthermophilic organism was more flexible than its mesophilic counterpart at both temperatures; however, the overall flexibility of both molecules at their optimal growth temperature was the same, despite 59% sequence homology. The conformational space sampled by both molecules was larger at 300 K than at 373 K. The essential dynamics analysis showed that the principal overall motions of the two molecules are significantly different. On the contrary, each molecule showed similar directions of motion at both temperatures. (C) 2002 Wiley-Liss, Inc.
Author Keywords:
essential dynamics, protein stability, thermostability, cooperativity, flexibility
KeyWords Plus:
ARCHAEBACTERIUM PYROCOCCUS-FURIOSUS, PROTEIN THERMOSTABILITY, STABILITY, SIMULATIONS, ACIDOCALDARIUS, TEMPERATURE, RESOLUTION, MECHANICS, SEQUENCES, INSIGHTS
Addresses:
Grottesi A, Univ Roma La Sapienza, Dept Chem, POB 34
Roma,62 Ple Aldo Moro 5, I-00185 Rome, Italy
Univ Roma La
Sapienza, Dept Chem, I-00185 Rome, Italy
Univ Roma La Sapienza,
Dept Biochem Sci, I-00185 Rome, Italy