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The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins
Proteins undergo both cold and heat denaturation, but often cold denaturation cannot be detected because it occurs at temperatures below water freezing. Proteins undergoing detectable cold as well as heat denaturation yield a reliable curve of protein stability. Here we use bacterial IscU, an essent...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7612454/ https://www.ncbi.nlm.nih.gov/pubmed/35243006 http://dx.doi.org/10.1038/s42004-018-0015-1 |
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author | Yan, Robert Rios, Paolo DeLos Pastore, Annalisa Temussi, Piero Andrea |
author_facet | Yan, Robert Rios, Paolo DeLos Pastore, Annalisa Temussi, Piero Andrea |
author_sort | Yan, Robert |
collection | PubMed |
description | Proteins undergo both cold and heat denaturation, but often cold denaturation cannot be detected because it occurs at temperatures below water freezing. Proteins undergoing detectable cold as well as heat denaturation yield a reliable curve of protein stability. Here we use bacterial IscU, an essential and ancient protein involved in iron cluster biogenesis, to show an important example of unbiased cold denaturation, based on electrostatic frustration caused by a dualism between iron–sulfur cluster binding and the presence of a functionally essential electrostatic gate. We explore the structural determinants and the universals that determine cold denaturation with the aid of a coarse grain model. Our results set a firm point in our understanding of cold denaturation and give us general rules to induce and predict protein cold denaturation. The conflict between ligand binding and stability hints at the importance of the structure–function dualism in protein evolution. |
format | Online Article Text |
id | pubmed-7612454 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
record_format | MEDLINE/PubMed |
spelling | pubmed-76124542022-03-02 The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins Yan, Robert Rios, Paolo DeLos Pastore, Annalisa Temussi, Piero Andrea Commun Chem Article Proteins undergo both cold and heat denaturation, but often cold denaturation cannot be detected because it occurs at temperatures below water freezing. Proteins undergoing detectable cold as well as heat denaturation yield a reliable curve of protein stability. Here we use bacterial IscU, an essential and ancient protein involved in iron cluster biogenesis, to show an important example of unbiased cold denaturation, based on electrostatic frustration caused by a dualism between iron–sulfur cluster binding and the presence of a functionally essential electrostatic gate. We explore the structural determinants and the universals that determine cold denaturation with the aid of a coarse grain model. Our results set a firm point in our understanding of cold denaturation and give us general rules to induce and predict protein cold denaturation. The conflict between ligand binding and stability hints at the importance of the structure–function dualism in protein evolution. 2018-04-05 /pmc/articles/PMC7612454/ /pubmed/35243006 http://dx.doi.org/10.1038/s42004-018-0015-1 Text en https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Yan, Robert Rios, Paolo DeLos Pastore, Annalisa Temussi, Piero Andrea The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins |
title | The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins |
title_full | The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins |
title_fullStr | The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins |
title_full_unstemmed | The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins |
title_short | The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins |
title_sort | cold denaturation of iscu highlights structure–function dualism in marginally stable proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7612454/ https://www.ncbi.nlm.nih.gov/pubmed/35243006 http://dx.doi.org/10.1038/s42004-018-0015-1 |
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