Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations
Candida antarctica lipase B (CALB) belongs to psychrophilic lipases which hydrolyze carboxyl ester bonds at low temperatures. There have been some features reported about cold-activity of the enzyme through experimental methods, whereas there is no detailed information on its mechanism of action at...
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ftpubmed:oai:pubmedcentral.nih.gov:3393743 2023-05-15T13:31:16+02:00 Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations Ganjalikhany, Mohamad Reza Ranjbar, Bijan Taghavi, Amir Hossein Tohidi Moghadam, Tahereh 2012-07-10 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3393743 http://www.ncbi.nlm.nih.gov/pubmed/22808134 https://doi.org/10.1371/journal.pone.0040327 en eng Public Library of Science http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3393743 http://www.ncbi.nlm.nih.gov/pubmed/22808134 http://dx.doi.org/10.1371/journal.pone.0040327 Ganjalikhany et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. CC-BY Research Article Text 2012 ftpubmed https://doi.org/10.1371/journal.pone.0040327 2013-09-04T09:54:51Z Candida antarctica lipase B (CALB) belongs to psychrophilic lipases which hydrolyze carboxyl ester bonds at low temperatures. There have been some features reported about cold-activity of the enzyme through experimental methods, whereas there is no detailed information on its mechanism of action at molecular level. Herein, a comparative molecular dynamics simulation and essential dynamics analysis have been carried out at three temperatures (5, 35 and 50°C) to trace the dominant factors in the psychrophilic properties of CALB under cold condition. The results clearly describe the effect of temperature on CALB with meaningful differences in the flexibility of the lid region (α5 helix), covering residues 141–147. Open- closed conformations have been obtained from different sets of long-term simulations (60 ns) at 5°C gave two reproducible distinct forms of CALB. The starting open conformation became closed immediately at 35 and 50°C during 60 ns of simulation, while a sequential open-closed form was observed at 5°C. These structural alterations were resulted from α5 helical movements, where the closed conformation of active site cleft was formed by displacement of both helix and its side chains. Analysis of normal mode showed concerted motions that are involved in the movement of both α5 and α10 helices. It is suggested that the functional motions needed for lypolytic activity of CALB is constructed from short-range movement of α5, accompanied by long-range movement of the domains connected to the lid region. Text Antarc* Antarctica PubMed Central (PMC) PLoS ONE 7 7 e40327 |
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Research Article Ganjalikhany, Mohamad Reza Ranjbar, Bijan Taghavi, Amir Hossein Tohidi Moghadam, Tahereh Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations |
topic_facet |
Research Article |
description |
Candida antarctica lipase B (CALB) belongs to psychrophilic lipases which hydrolyze carboxyl ester bonds at low temperatures. There have been some features reported about cold-activity of the enzyme through experimental methods, whereas there is no detailed information on its mechanism of action at molecular level. Herein, a comparative molecular dynamics simulation and essential dynamics analysis have been carried out at three temperatures (5, 35 and 50°C) to trace the dominant factors in the psychrophilic properties of CALB under cold condition. The results clearly describe the effect of temperature on CALB with meaningful differences in the flexibility of the lid region (α5 helix), covering residues 141–147. Open- closed conformations have been obtained from different sets of long-term simulations (60 ns) at 5°C gave two reproducible distinct forms of CALB. The starting open conformation became closed immediately at 35 and 50°C during 60 ns of simulation, while a sequential open-closed form was observed at 5°C. These structural alterations were resulted from α5 helical movements, where the closed conformation of active site cleft was formed by displacement of both helix and its side chains. Analysis of normal mode showed concerted motions that are involved in the movement of both α5 and α10 helices. It is suggested that the functional motions needed for lypolytic activity of CALB is constructed from short-range movement of α5, accompanied by long-range movement of the domains connected to the lid region. |
format |
Text |
author |
Ganjalikhany, Mohamad Reza Ranjbar, Bijan Taghavi, Amir Hossein Tohidi Moghadam, Tahereh |
author_facet |
Ganjalikhany, Mohamad Reza Ranjbar, Bijan Taghavi, Amir Hossein Tohidi Moghadam, Tahereh |
author_sort |
Ganjalikhany, Mohamad Reza |
title |
Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations |
title_short |
Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations |
title_full |
Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations |
title_fullStr |
Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations |
title_full_unstemmed |
Functional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations |
title_sort |
functional motions of candida antarctica lipase b: a survey through open-close conformations |
publisher |
Public Library of Science |
publishDate |
2012 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3393743 http://www.ncbi.nlm.nih.gov/pubmed/22808134 https://doi.org/10.1371/journal.pone.0040327 |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3393743 http://www.ncbi.nlm.nih.gov/pubmed/22808134 http://dx.doi.org/10.1371/journal.pone.0040327 |
op_rights |
Ganjalikhany et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
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CC-BY |
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https://doi.org/10.1371/journal.pone.0040327 |
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PLoS ONE |
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7 |
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e40327 |
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1766017111401955328 |