Protein flexibility in psychrophilic and mesophilic trypsins. Evidence of evolutionary conservation of protein dynamics in trypsin-like serine-proteases.
To shed light on the molecular features related to cold-adaptation in serine-proteases, we have carried out molecular dynamics simulations of homologous mesophilic and psychrophilic trypsins, with particular attention to evaluation of intramolecular interactions and flexibility. Psychrophilic trypsins present fewer interdomain interactions and enhanced localized flexibility in regions close to the catalytic site. Notably, these regions fit well with the pattern of protein flexibility previously reported for psychrophilic elastases. Our results indicate that specific sites within the serine-protease fold can be considered hot spots of cold-adaptation and that psychrophilic trypsins and elastases have independently discovered similar molecular strategies to optimize flexibility at low temperatures.
Papaleo
Elena
E
Department of Biotechnology and Bioscience, University of Milano-Bicocca, 20126 Milan, Italy. elena.papaleo@unimib.it <elena.papaleo@unimib.it>
Pasi
Marco
M
Riccardi
Laura
L
Sambi
Ilaria
I
Fantucci
Piercarlo
P
De Gioia
Luca
L
D000818:Animals; D003080:Cold Temperature; D019143:Evolution, Molecular; D006801:Humans; D010802:Phylogeny; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000145:classification*
C114880:trypsin-like serine protease; D012697:Serine Endopeptidases