Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases
Adaptation to both high and low temperatures requires proteins with special properties. While organisms living at or close to the boiling point of water need to have proteins with increased stability, other properties are required at temperatures close to the freezing point of water. Indeed, it has...
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ftunivmilanobic:oai:boa.unimib.it:10281/14034 2024-04-14T08:09:18+00:00 Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases PAPALEO, ELENA DE GIOIA, LUCA Olufsen, M Brandsdal, BO Papaleo, E Olufsen, M DE GIOIA, L Brandsdal, B 2007 http://hdl.handle.net/10281/14034 https://doi.org/10.1016/j.jmgm.2006.09.012 eng eng Elsevier info:eu-repo/semantics/altIdentifier/pmid/17084098 info:eu-repo/semantics/altIdentifier/wos/WOS:000248646500009 volume:26 issue:1 firstpage:93 lastpage:103 journal:JOURNAL OF MOLECULAR GRAPHICS & MODELLING http://hdl.handle.net/10281/14034 doi:10.1016/j.jmgm.2006.09.012 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34347235460 protein chemistry info:eu-repo/semantics/article 2007 ftunivmilanobic https://doi.org/10.1016/j.jmgm.2006.09.012 2024-03-21T16:31:54Z Adaptation to both high and low temperatures requires proteins with special properties. While organisms living at or close to the boiling point of water need to have proteins with increased stability, other properties are required at temperatures close to the freezing point of water. Indeed, it has been shown that enzymes adapted to cold environments are less resistant to heat with a concomitant increased activity as compared to their warm-active counter-parts. Several recent studies have pointed in the direction that electrostatic interactions play a central role in temperature adaptation, and in this study we investigate the role such interactions have in adaptation of elastase from Atlantic salmon and pig. Molecular dynamics (MD) simulations have been used to generate structural ensembles at 283 and 310 K of the psychrophilic and mesophilic elastase, and a total of eight 12 ns simulations have been carried out. Even though the two homologues have a highly similar three-dimensional structure, the location and number of charged amino acids are very different. Based on the simulated structures we find that very few salt-bridges are stable throughout the simulations, and provide little stabilization/destabilization of the proteins as judged by continuum electrostatic calculations. However, the mesophilic elastase is characterized by a greater number of salt-bridges as well as a putative salt-bridge network close to the catalytic site, indicating a higher rigidity of the components involved in the catalytic cycle. In addition, subtle differences are also found in the electrostatic potentials in the vicinity of the catalytic residues, which may explain the increased catalytic efficiency of the cold-adapted elastase. © 2006 Elsevier Inc. All rights reserved. Article in Journal/Newspaper Atlantic salmon Università degli Studi di Milano-Bicocca: BOA (Bicocca Open Archive) Journal of Molecular Graphics and Modelling 26 1 93 103 |
institution |
Open Polar |
collection |
Università degli Studi di Milano-Bicocca: BOA (Bicocca Open Archive) |
op_collection_id |
ftunivmilanobic |
language |
English |
topic |
protein chemistry |
spellingShingle |
protein chemistry PAPALEO, ELENA DE GIOIA, LUCA Olufsen, M Brandsdal, BO Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases |
topic_facet |
protein chemistry |
description |
Adaptation to both high and low temperatures requires proteins with special properties. While organisms living at or close to the boiling point of water need to have proteins with increased stability, other properties are required at temperatures close to the freezing point of water. Indeed, it has been shown that enzymes adapted to cold environments are less resistant to heat with a concomitant increased activity as compared to their warm-active counter-parts. Several recent studies have pointed in the direction that electrostatic interactions play a central role in temperature adaptation, and in this study we investigate the role such interactions have in adaptation of elastase from Atlantic salmon and pig. Molecular dynamics (MD) simulations have been used to generate structural ensembles at 283 and 310 K of the psychrophilic and mesophilic elastase, and a total of eight 12 ns simulations have been carried out. Even though the two homologues have a highly similar three-dimensional structure, the location and number of charged amino acids are very different. Based on the simulated structures we find that very few salt-bridges are stable throughout the simulations, and provide little stabilization/destabilization of the proteins as judged by continuum electrostatic calculations. However, the mesophilic elastase is characterized by a greater number of salt-bridges as well as a putative salt-bridge network close to the catalytic site, indicating a higher rigidity of the components involved in the catalytic cycle. In addition, subtle differences are also found in the electrostatic potentials in the vicinity of the catalytic residues, which may explain the increased catalytic efficiency of the cold-adapted elastase. © 2006 Elsevier Inc. All rights reserved. |
author2 |
Papaleo, E Olufsen, M DE GIOIA, L Brandsdal, B |
format |
Article in Journal/Newspaper |
author |
PAPALEO, ELENA DE GIOIA, LUCA Olufsen, M Brandsdal, BO |
author_facet |
PAPALEO, ELENA DE GIOIA, LUCA Olufsen, M Brandsdal, BO |
author_sort |
PAPALEO, ELENA |
title |
Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases |
title_short |
Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases |
title_full |
Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases |
title_fullStr |
Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases |
title_full_unstemmed |
Optimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastases |
title_sort |
optimization of electrostatics as a strategy for cold-adaptation: a case study of cold- and warm-active elastases |
publisher |
Elsevier |
publishDate |
2007 |
url |
http://hdl.handle.net/10281/14034 https://doi.org/10.1016/j.jmgm.2006.09.012 |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/17084098 info:eu-repo/semantics/altIdentifier/wos/WOS:000248646500009 volume:26 issue:1 firstpage:93 lastpage:103 journal:JOURNAL OF MOLECULAR GRAPHICS & MODELLING http://hdl.handle.net/10281/14034 doi:10.1016/j.jmgm.2006.09.012 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34347235460 |
op_doi |
https://doi.org/10.1016/j.jmgm.2006.09.012 |
container_title |
Journal of Molecular Graphics and Modelling |
container_volume |
26 |
container_issue |
1 |
container_start_page |
93 |
op_container_end_page |
103 |
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1796306800101818368 |