Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation
The present paper reports structure prediction and analysis of a psychrophilic β-mannanase from Glaciozyma antarctica PI12 yeast. A threading method was used for 3D structure prediction of the enzyme using the MODELLER 9v12 program regarding its low sequence identity (<30%). The constructed model...
Published in: | Molecular Simulation |
---|---|
Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
Taylor & Francis Group
2018
|
Subjects: | |
Online Access: | http://eprints.utm.my/84269/ https://doi.org/10.1080/08927022.2018.1492721 |
id |
ftunivmalaysia:oai:generic.eprints.org:84269 |
---|---|
record_format |
openpolar |
spelling |
ftunivmalaysia:oai:generic.eprints.org:84269 2023-11-12T04:03:57+01:00 Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation Parvizpour, Sepideh Razmara, Jafar Shamsir, Mohd. Shahir 2018 http://eprints.utm.my/84269/ https://doi.org/10.1080/08927022.2018.1492721 unknown Taylor & Francis Group Parvizpour, Sepideh and Razmara, Jafar and Shamsir, Mohd. Shahir (2018) Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation. Molecular Simulation, 44 (15). pp. 1270-1277. ISSN 0892-7022 TP Chemical technology Article PeerReviewed 2018 ftunivmalaysia https://doi.org/10.1080/08927022.2018.1492721 2023-10-24T18:02:14Z The present paper reports structure prediction and analysis of a psychrophilic β-mannanase from Glaciozyma antarctica PI12 yeast. A threading method was used for 3D structure prediction of the enzyme using the MODELLER 9v12 program regarding its low sequence identity (<30%). The constructed model has been used in a comparative study to analyse its cold adaptation mechanism using other mesophilic, thermophilic, and hyperthermophilic mannanases. The structural and molecular dynamics analysis suggests that flexibility of the enzyme is increased through different structural characteristics, and therefore, the possibility of efficient catalytic reactions is provided at cold environment. These characteristics are the presence of longer loops, broken or shorter strands and helices, a lower number of salt bridges and hydrogen bonds, a higher exposure of the hydrophobic side chains to the solvent and an increased total solvent accessible surface area. Furthermore, the high catalytic efficiency and structural flexibility of the psychrophilic mannanase was supported by the results of principal component analysis. Article in Journal/Newspaper Antarc* Antarctica Universiti Teknologi Malaysia: Institutional Repository Molecular Simulation 44 15 1270 1277 |
institution |
Open Polar |
collection |
Universiti Teknologi Malaysia: Institutional Repository |
op_collection_id |
ftunivmalaysia |
language |
unknown |
topic |
TP Chemical technology |
spellingShingle |
TP Chemical technology Parvizpour, Sepideh Razmara, Jafar Shamsir, Mohd. Shahir Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
topic_facet |
TP Chemical technology |
description |
The present paper reports structure prediction and analysis of a psychrophilic β-mannanase from Glaciozyma antarctica PI12 yeast. A threading method was used for 3D structure prediction of the enzyme using the MODELLER 9v12 program regarding its low sequence identity (<30%). The constructed model has been used in a comparative study to analyse its cold adaptation mechanism using other mesophilic, thermophilic, and hyperthermophilic mannanases. The structural and molecular dynamics analysis suggests that flexibility of the enzyme is increased through different structural characteristics, and therefore, the possibility of efficient catalytic reactions is provided at cold environment. These characteristics are the presence of longer loops, broken or shorter strands and helices, a lower number of salt bridges and hydrogen bonds, a higher exposure of the hydrophobic side chains to the solvent and an increased total solvent accessible surface area. Furthermore, the high catalytic efficiency and structural flexibility of the psychrophilic mannanase was supported by the results of principal component analysis. |
format |
Article in Journal/Newspaper |
author |
Parvizpour, Sepideh Razmara, Jafar Shamsir, Mohd. Shahir |
author_facet |
Parvizpour, Sepideh Razmara, Jafar Shamsir, Mohd. Shahir |
author_sort |
Parvizpour, Sepideh |
title |
Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
title_short |
Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
title_full |
Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
title_fullStr |
Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
title_full_unstemmed |
Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
title_sort |
temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation |
publisher |
Taylor & Francis Group |
publishDate |
2018 |
url |
http://eprints.utm.my/84269/ https://doi.org/10.1080/08927022.2018.1492721 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
Parvizpour, Sepideh and Razmara, Jafar and Shamsir, Mohd. Shahir (2018) Temperature adaptation analysis of a psychrophilic mannanase through structural, functional and molecular dynamics simulation. Molecular Simulation, 44 (15). pp. 1270-1277. ISSN 0892-7022 |
op_doi |
https://doi.org/10.1080/08927022.2018.1492721 |
container_title |
Molecular Simulation |
container_volume |
44 |
container_issue |
15 |
container_start_page |
1270 |
op_container_end_page |
1277 |
_version_ |
1782339885630226432 |