Water stabilizes an alternate turn conformation in horse heart myoglobin

Comparison of myoglobin structures reveals that protein isolated from horse heart consistently adopts an alternate turn conformation in comparison to its homologues. Analysis of hundreds of high-resolution structures discounts crystallization conditions or the surrounding amino acid protein environm...

Descripción completa

Detalles Bibliográficos
Autores principales: Bronstein, Alex, Marx, Ailie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10102282/
https://www.ncbi.nlm.nih.gov/pubmed/37055458
http://dx.doi.org/10.1038/s41598-023-32821-z
_version_ 1785025659768143872
author Bronstein, Alex
Marx, Ailie
author_facet Bronstein, Alex
Marx, Ailie
author_sort Bronstein, Alex
collection PubMed
description Comparison of myoglobin structures reveals that protein isolated from horse heart consistently adopts an alternate turn conformation in comparison to its homologues. Analysis of hundreds of high-resolution structures discounts crystallization conditions or the surrounding amino acid protein environment as explaining this difference, that is also not captured by the AlphaFold prediction. Rather, a water molecule is identified as stabilizing the conformation in the horse heart structure, which immediately reverts to the whale conformation in molecular dynamics simulations excluding that structural water.
format Online
Article
Text
id pubmed-10102282
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-101022822023-04-15 Water stabilizes an alternate turn conformation in horse heart myoglobin Bronstein, Alex Marx, Ailie Sci Rep Article Comparison of myoglobin structures reveals that protein isolated from horse heart consistently adopts an alternate turn conformation in comparison to its homologues. Analysis of hundreds of high-resolution structures discounts crystallization conditions or the surrounding amino acid protein environment as explaining this difference, that is also not captured by the AlphaFold prediction. Rather, a water molecule is identified as stabilizing the conformation in the horse heart structure, which immediately reverts to the whale conformation in molecular dynamics simulations excluding that structural water. Nature Publishing Group UK 2023-04-13 /pmc/articles/PMC10102282/ /pubmed/37055458 http://dx.doi.org/10.1038/s41598-023-32821-z Text en © The Author(s) 2023 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Bronstein, Alex
Marx, Ailie
Water stabilizes an alternate turn conformation in horse heart myoglobin
title Water stabilizes an alternate turn conformation in horse heart myoglobin
title_full Water stabilizes an alternate turn conformation in horse heart myoglobin
title_fullStr Water stabilizes an alternate turn conformation in horse heart myoglobin
title_full_unstemmed Water stabilizes an alternate turn conformation in horse heart myoglobin
title_short Water stabilizes an alternate turn conformation in horse heart myoglobin
title_sort water stabilizes an alternate turn conformation in horse heart myoglobin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10102282/
https://www.ncbi.nlm.nih.gov/pubmed/37055458
http://dx.doi.org/10.1038/s41598-023-32821-z
work_keys_str_mv AT bronsteinalex waterstabilizesanalternateturnconformationinhorseheartmyoglobin
AT marxailie waterstabilizesanalternateturnconformationinhorseheartmyoglobin

Ejemplares similares