The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus
Tetrameric hemoglobins (Hbs) are prototypical systems for the investigations of fundamental properties of proteins. Although the structure of these proteins has been known for nearly sixty years, there are many aspects related to their function/structure that are still obscure. Here, we report the c...
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ftpubmed:oai:pubmedcentral.nih.gov:6908587 2023-05-15T13:43:29+02:00 The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus Balasco, Nicole Vitagliano, Luigi Merlino, Antonello Verde, Cinzia Mazzarella, Lelio Vergara, Alessandro 2019-12-12 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6908587/ http://www.ncbi.nlm.nih.gov/pubmed/31831781 https://doi.org/10.1038/s41598-019-55331-3 en eng Nature Publishing Group UK http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6908587/ http://www.ncbi.nlm.nih.gov/pubmed/31831781 http://dx.doi.org/10.1038/s41598-019-55331-3 © The Author(s) 2019 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 http://creativecommons.org/licenses/by/4.0/. CC-BY Article Text 2019 ftpubmed https://doi.org/10.1038/s41598-019-55331-3 2019-12-22T01:25:43Z Tetrameric hemoglobins (Hbs) are prototypical systems for the investigations of fundamental properties of proteins. Although the structure of these proteins has been known for nearly sixty years, there are many aspects related to their function/structure that are still obscure. Here, we report the crystal structure of a carbonmonoxy form of the Hb isolated from the sub-Antarctic notothenioid fish Eleginops maclovinus characterised by either rare or unique features. In particular, the distal site of the α chain results to be very unusual since the distal His is displaced from its canonical position. This displacement is coupled with a shortening of the highly conserved E helix and the formation of novel interactions at tertiary structure level. Interestingly, the quaternary structure is closer to the T-deoxy state of Hbs than to the R-state despite the full coordination of all chains. Notably, these peculiar structural features provide a rationale for some spectroscopic properties exhibited by the protein in solution. Finally, this unexpected structural plasticity of the heme distal side has been associated with specific sequence signatures of various Hbs. Text Antarc* Antarctic PubMed Central (PMC) Antarctic Scientific Reports 9 1 |
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Article Balasco, Nicole Vitagliano, Luigi Merlino, Antonello Verde, Cinzia Mazzarella, Lelio Vergara, Alessandro The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus |
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Tetrameric hemoglobins (Hbs) are prototypical systems for the investigations of fundamental properties of proteins. Although the structure of these proteins has been known for nearly sixty years, there are many aspects related to their function/structure that are still obscure. Here, we report the crystal structure of a carbonmonoxy form of the Hb isolated from the sub-Antarctic notothenioid fish Eleginops maclovinus characterised by either rare or unique features. In particular, the distal site of the α chain results to be very unusual since the distal His is displaced from its canonical position. This displacement is coupled with a shortening of the highly conserved E helix and the formation of novel interactions at tertiary structure level. Interestingly, the quaternary structure is closer to the T-deoxy state of Hbs than to the R-state despite the full coordination of all chains. Notably, these peculiar structural features provide a rationale for some spectroscopic properties exhibited by the protein in solution. Finally, this unexpected structural plasticity of the heme distal side has been associated with specific sequence signatures of various Hbs. |
format |
Text |
author |
Balasco, Nicole Vitagliano, Luigi Merlino, Antonello Verde, Cinzia Mazzarella, Lelio Vergara, Alessandro |
author_facet |
Balasco, Nicole Vitagliano, Luigi Merlino, Antonello Verde, Cinzia Mazzarella, Lelio Vergara, Alessandro |
author_sort |
Balasco, Nicole |
title |
The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus |
title_short |
The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus |
title_full |
The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus |
title_fullStr |
The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus |
title_full_unstemmed |
The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus |
title_sort |
unique structural features of carbonmonoxy hemoglobin from the sub-antarctic fish eleginops maclovinus |
publisher |
Nature Publishing Group UK |
publishDate |
2019 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6908587/ http://www.ncbi.nlm.nih.gov/pubmed/31831781 https://doi.org/10.1038/s41598-019-55331-3 |
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Antarctic |
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Antarctic |
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Antarc* Antarctic |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6908587/ http://www.ncbi.nlm.nih.gov/pubmed/31831781 http://dx.doi.org/10.1038/s41598-019-55331-3 |
op_rights |
© The Author(s) 2019 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 http://creativecommons.org/licenses/by/4.0/. |
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CC-BY |
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https://doi.org/10.1038/s41598-019-55331-3 |
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Scientific Reports |
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