Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures.
Molecular Dynamics (MD) simulations have been used to understand how protein structure, dynamics, and flexibility are affected by adaptation to high temperature for several years. We report here the results of the high temperature MD simulations of Bacillus stearothermophilus L1 (L1 lipase). We foun...
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| Format: | Article |
| Language: | English English |
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Springer
2009
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| Online Access: | http://psasir.upm.edu.my/id/eprint/15706/ http://psasir.upm.edu.my/id/eprint/15706/1/Molecular%20dynamics%20study%20of%20the%20structure.pdf |
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| author | Abedi Karjiban, Roghayeh Abdul Rahman, Mohd Basyaruddin Basri, Mahiran Salleh, Abu Bakar Jacobs, Donald Abdul Wahab, Habibah |
| author_facet | Abedi Karjiban, Roghayeh Abdul Rahman, Mohd Basyaruddin Basri, Mahiran Salleh, Abu Bakar Jacobs, Donald Abdul Wahab, Habibah |
| author_sort | Abedi Karjiban, Roghayeh |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Molecular Dynamics (MD) simulations have been used to understand how protein structure, dynamics, and flexibility are affected by adaptation to high temperature for several years. We report here the results of the high temperature MD simulations of Bacillus stearothermophilus L1 (L1 lipase). We found that the N-terminal moiety of the enzyme showed a high flexibility and dynamics during high temperature simulations which preceded and followed by clear structural changes in two specific regions; the small domain and the main catalytic domain or core domain of the enzyme. These two domains interact with each other through a Zn(2+)-binding coordination with Asp-61 and Asp-238 from the core domain and His-81 and His-87 from the small domain. Interestingly, the His-81 and His-87 were among the highly fluctuated and mobile residues at high temperatures. The results appear to suggest that tight interactions of Zn(2+)-binding coordination with specified residues became weak at high temperature which suggests the contribution of this region to the thermostability of the enzyme. |
| first_indexed | 2025-11-15T08:04:09Z |
| format | Article |
| id | upm-15706 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English English |
| last_indexed | 2025-11-15T08:04:09Z |
| publishDate | 2009 |
| publisher | Springer |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-157062015-11-25T04:49:20Z http://psasir.upm.edu.my/id/eprint/15706/ Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. Abedi Karjiban, Roghayeh Abdul Rahman, Mohd Basyaruddin Basri, Mahiran Salleh, Abu Bakar Jacobs, Donald Abdul Wahab, Habibah Molecular Dynamics (MD) simulations have been used to understand how protein structure, dynamics, and flexibility are affected by adaptation to high temperature for several years. We report here the results of the high temperature MD simulations of Bacillus stearothermophilus L1 (L1 lipase). We found that the N-terminal moiety of the enzyme showed a high flexibility and dynamics during high temperature simulations which preceded and followed by clear structural changes in two specific regions; the small domain and the main catalytic domain or core domain of the enzyme. These two domains interact with each other through a Zn(2+)-binding coordination with Asp-61 and Asp-238 from the core domain and His-81 and His-87 from the small domain. Interestingly, the His-81 and His-87 were among the highly fluctuated and mobile residues at high temperatures. The results appear to suggest that tight interactions of Zn(2+)-binding coordination with specified residues became weak at high temperature which suggests the contribution of this region to the thermostability of the enzyme. Springer 2009 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/15706/1/Molecular%20dynamics%20study%20of%20the%20structure.pdf Abedi Karjiban, Roghayeh and Abdul Rahman, Mohd Basyaruddin and Basri, Mahiran and Salleh, Abu Bakar and Jacobs, Donald and Abdul Wahab, Habibah (2009) Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. The Protein Journal, 28 (1). pp. 14-23. ISSN 1573-4943 Thermostat Lipase Molecular dynamics 10.1007/s10930-008-9159-7 English |
| spellingShingle | Thermostat Lipase Molecular dynamics Abedi Karjiban, Roghayeh Abdul Rahman, Mohd Basyaruddin Basri, Mahiran Salleh, Abu Bakar Jacobs, Donald Abdul Wahab, Habibah Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. |
| title | Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. |
| title_full | Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. |
| title_fullStr | Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. |
| title_full_unstemmed | Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. |
| title_short | Molecular dynamics study of the structure, flexibility and dynamics of thermostable L1 lipase at high temperatures. |
| title_sort | molecular dynamics study of the structure, flexibility and dynamics of thermostable l1 lipase at high temperatures. |
| topic | Thermostat Lipase Molecular dynamics |
| url | http://psasir.upm.edu.my/id/eprint/15706/ http://psasir.upm.edu.my/id/eprint/15706/ http://psasir.upm.edu.my/id/eprint/15706/1/Molecular%20dynamics%20study%20of%20the%20structure.pdf |