Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling
Abstract Rational design of functional enzymes is a powerful strategy to gain deep insights into more complex native enzymes, such as nitric oxide reductase (NOR). Recently, we engineered a functional model of NOR by creating a two His and one Glu (2‐His‐1‐Glu) non‐heme iron center in sperm whale my...
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crwiley:10.1002/prot.22928 2024-06-02T08:14:53+00:00 Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling Lin, Ying‐Wu 2010 http://dx.doi.org/10.1002/prot.22928 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.22928 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.22928 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Proteins: Structure, Function, and Bioinformatics volume 79, issue 3, page 679-684 ISSN 0887-3585 1097-0134 journal-article 2010 crwiley https://doi.org/10.1002/prot.22928 2024-05-03T11:48:17Z Abstract Rational design of functional enzymes is a powerful strategy to gain deep insights into more complex native enzymes, such as nitric oxide reductase (NOR). Recently, we engineered a functional model of NOR by creating a two His and one Glu (2‐His‐1‐Glu) non‐heme iron center in sperm whale myoglobin (swMb L29E, F43H, H64, called Fe B Mb(‐His)). It was found that Fe B Mb(‐His) adopts a low‐spin state with bis‐His coordination in the absence of metal ions binding to the designed metal center. However, no structural information was available for the variant in this special spin state. We herein performed molecular modeling of Fe B Mb(‐His) and compared with the X‐ray structure of its copper bound derivative, Cu(II)‐CN − ‐Fe B Mb(‐His), resolved recently at a high resolution (1.65 Å) (PDB entry 3MN0). The simulated structure shows that mutation of Leu to Glu at position 29 in the hydrophobic heme pocket alters the folding behavior of Mb. The hydrogen bond between Glu29 and His64 further plays a role in stabilizing the bis‐His (His64/His93) coordination structure. This study offers an excellent example of using molecular modeling to gain insights in rational design of both structural and functional proteins. Proteins 2011. © 2010 Wiley‐Liss, Inc. Article in Journal/Newspaper Sperm whale Wiley Online Library Proteins: Structure, Function, and Bioinformatics 79 3 679 684 |
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English |
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Abstract Rational design of functional enzymes is a powerful strategy to gain deep insights into more complex native enzymes, such as nitric oxide reductase (NOR). Recently, we engineered a functional model of NOR by creating a two His and one Glu (2‐His‐1‐Glu) non‐heme iron center in sperm whale myoglobin (swMb L29E, F43H, H64, called Fe B Mb(‐His)). It was found that Fe B Mb(‐His) adopts a low‐spin state with bis‐His coordination in the absence of metal ions binding to the designed metal center. However, no structural information was available for the variant in this special spin state. We herein performed molecular modeling of Fe B Mb(‐His) and compared with the X‐ray structure of its copper bound derivative, Cu(II)‐CN − ‐Fe B Mb(‐His), resolved recently at a high resolution (1.65 Å) (PDB entry 3MN0). The simulated structure shows that mutation of Leu to Glu at position 29 in the hydrophobic heme pocket alters the folding behavior of Mb. The hydrogen bond between Glu29 and His64 further plays a role in stabilizing the bis‐His (His64/His93) coordination structure. This study offers an excellent example of using molecular modeling to gain insights in rational design of both structural and functional proteins. Proteins 2011. © 2010 Wiley‐Liss, Inc. |
format |
Article in Journal/Newspaper |
author |
Lin, Ying‐Wu |
spellingShingle |
Lin, Ying‐Wu Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
author_facet |
Lin, Ying‐Wu |
author_sort |
Lin, Ying‐Wu |
title |
Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
title_short |
Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
title_full |
Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
title_fullStr |
Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
title_full_unstemmed |
Structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
title_sort |
structural insights into a low‐spin myoglobin variant with bis‐histidine coordination from molecular modeling |
publisher |
Wiley |
publishDate |
2010 |
url |
http://dx.doi.org/10.1002/prot.22928 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.22928 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.22928 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Proteins: Structure, Function, and Bioinformatics volume 79, issue 3, page 679-684 ISSN 0887-3585 1097-0134 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/prot.22928 |
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Proteins: Structure, Function, and Bioinformatics |
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79 |
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3 |
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679 |
op_container_end_page |
684 |
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1800738898055266304 |