caa a22 4500 605511861 CHVBK 20210128100653.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00894-015-2617-1 doi (NATIONALLICENCE)springer-10.1007/s00894-015-2617-1 Structural prediction of a novel laminarinase from the psychrophilic Glaciozyma antarctica PI12 and its temperature adaptation analysis [Elektronische Daten] [Sepideh Parvizpour, Jafar Razmara, Ashraf Jomah, Mohd Shamsir, Rosli Illias] Here, we present a novel psychrophilic β-glucanase from Glaciozyma antarctica PI12 yeast that has been structurally modeled and analyzed in detail. To our knowledge, this is the first attempt to model a psychrophilic laminarinase from yeast. Because of the low sequence identity (<40%), a threading method was applied to predict a 3D structure of the enzyme using the MODELLER9v12 program. The results of a comparative study using other mesophilic, thermophilic, and hyperthermophilic laminarinases indicated several amino acid substitutions on the surface of psychrophilic laminarinase that totally increased the flexibility of its structure for efficient catalytic reactions at low temperatures. Whereas several structural factors in the overall structure can explain the weak thermal stability, this research suggests that the psychrophilic adaptation and catalytic activity at low temperatures were achieved through existence of longer loops and shorter or broken helices and strands, an increase in the number of aromatic and hydrophobic residues, a reduction in the number of hydrogen bonds and salt bridges, a higher total solvent accessible surface area, and an increase in the exposure of the hydrophobic side chains to the solvent. The results of comparative molecular dynamics simulation and principal component analysis confirmed the above strategies adopted by psychrophilic laminarinase to increase its catalytic efficiency and structural flexibility to be active at cold temperature. Graphical Abstract Structural prediction of a novel laminarinase from the psychrophilic Glaciozyma antarctica PI1ᅟ Springer-Verlag Berlin Heidelberg, 2015 Cold adaptation nationallicence Flexibility nationallicence Laminarinase nationallicence Psychrophile nationallicence Structure prediction nationallicence Parvizpour Sepideh Bioinformatics Research Group, Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut Razmara Jafar Department of Computer Sciences, University of Tabriz, Tabriz, Iran aut Jomah Ashraf Bioinformatics Research Group, Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut Shamsir Mohd Bioinformatics Research Group, Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut Illias Rosli Department of Bioprocess Engineering, Faculty of Chemical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut Journal of Molecular Modeling Springer Berlin Heidelberg 21/3(2015-03-01), 1-14 1610-2940 21:3<1 2015 21 894 https://doi.org/10.1007/s00894-015-2617-1 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00894-015-2617-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Parvizpour Sepideh Bioinformatics Research Group, Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut NATIONALLICENCE 700 1- Razmara Jafar Department of Computer Sciences, University of Tabriz, Tabriz, Iran aut NATIONALLICENCE 700 1- Jomah Ashraf Bioinformatics Research Group, Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut NATIONALLICENCE 700 1- Shamsir Mohd Bioinformatics Research Group, Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut NATIONALLICENCE 700 1- Illias Rosli Department of Bioprocess Engineering, Faculty of Chemical Engineering, Universiti Teknologi Malaysia, Johor, Malaysia aut NATIONALLICENCE 773 0- Journal of Molecular Modeling Springer Berlin Heidelberg 21/3(2015-03-01), 1-14 1610-2940 21:3<1 2015 21 894