Deciphering the flexibility and dynamics of Geobacillus zalihae strain T1 lipase at high temperatures by molecular dynamics simulation.
The stability of biocatalysts is an important criterion for a sustainable industrial operation economically. T1 lipase is a thermoalkalophilic enzyme derived from Geobacillus zalihae strain T1 (T1 lipase) that was isolated from palm oil mill effluent (POME) in Malaysia. We report here the results of high temperatures molecular dynamics (MD) simulations of T1 lipase in explicit solvent. We found that the N-terminal moiety of this enzyme was accompanied by a large flexibility and dynamics during temperature-induced unfolding simulations which preceded and followed by clear structural changes in two specific regions; the small domain (consisting of helices alpha3 and alpha5, strands beta1 and beta2, and connecting loops) and the main catalytic domain or core domain (consisting of helices alpha6- alpha9 and connecting loops which located above the active site) of the enzyme. The results suggest that the small domain of model enzyme is a critical region to the thermostability of this organism.
Abdul Rahman
Mohd Basyaruddin
MB
Structural Biology Research Centre, Malaysia Genome Institute, 43600 UKM Bangi, Selangor, Malaysia. basya@science.upm.edu.my
Karjiban
Roghayeh Abedi
RA
Salleh
Abu Bakar
AB
Jacobs
Donald
D
Basri
Mahiran
M
Thean Chor
Adam Leow
AL
Abdul Wahab
Habibah
H
Rahman
Raja Noor Zaliha Raja Abd
RN
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D056506:Geobacillus / Q000201:enzymology*; D006358:Hot Temperature; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012984:Software
D001426:Bacterial Proteins; D008049:Lipase