Crystal structure of the carbon monoxide complex of human cytoglobin
Abstract Cytoglobin (Cgb) is a vertebrate heme‐containing globin‐protein expressed in a broad range of mammalian tissues. Unlike myoglobin, Cgb displays a hexa‐coordinated (bis‐hystidyl) heme iron atom, having the heme distal His81(E7) residue as the endogenous sixth ligand. In the present study, we...
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crwiley:10.1002/prot.22950 2024-06-02T08:14:53+00:00 Crystal structure of the carbon monoxide complex of human cytoglobin Makino, Masatomo Sawai, Hitomi Shiro, Yoshitsugu Sugimoto, Hiroshi 2011 http://dx.doi.org/10.1002/prot.22950 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.22950 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.22950 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Proteins: Structure, Function, and Bioinformatics volume 79, issue 4, page 1143-1153 ISSN 0887-3585 1097-0134 journal-article 2011 crwiley https://doi.org/10.1002/prot.22950 2024-05-03T11:14:48Z Abstract Cytoglobin (Cgb) is a vertebrate heme‐containing globin‐protein expressed in a broad range of mammalian tissues. Unlike myoglobin, Cgb displays a hexa‐coordinated (bis‐hystidyl) heme iron atom, having the heme distal His81(E7) residue as the endogenous sixth ligand. In the present study, we crystallized human Cgb in the presence of a reductant Na 2 S 2 O 4 under a carbon monoxide (CO) atmosphere, and determined the crystal structure at 2.6 Å resolution. The CO ligand occupies the sixth axial position of the heme ferrous iron. Eventually, the imidazole group of His81(E7) is expelled from the sixth position and swings out of the distal heme pocket. The flipping motion of the His81 imidazole group accompanies structural readjustments of some residues (Gln62, Phe63, Gln72, and Ser75) in both the CD‐corner and D‐helix regions of Cgb. On the other hand, no significant structural changes were observed in other Cgb regions, for example, on the proximal side. These structural alterations that occurred as a result of exogenous ligand (CO) binding are clearly different from those observed in other vertebrate hexa‐coordinated globins (mouse neuroglobin, Drosophila melanogaster hemoglobin) and penta‐coordinated sperm whale myoglobin. The present study provides the structural basis for further discussion of the unique ligand‐binding properties of Cgb. Proteins 2011. © 2011 Wiley‐Liss, Inc. Article in Journal/Newspaper Sperm whale Wiley Online Library Proteins: Structure, Function, and Bioinformatics 79 4 1143 1153 |
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English |
description |
Abstract Cytoglobin (Cgb) is a vertebrate heme‐containing globin‐protein expressed in a broad range of mammalian tissues. Unlike myoglobin, Cgb displays a hexa‐coordinated (bis‐hystidyl) heme iron atom, having the heme distal His81(E7) residue as the endogenous sixth ligand. In the present study, we crystallized human Cgb in the presence of a reductant Na 2 S 2 O 4 under a carbon monoxide (CO) atmosphere, and determined the crystal structure at 2.6 Å resolution. The CO ligand occupies the sixth axial position of the heme ferrous iron. Eventually, the imidazole group of His81(E7) is expelled from the sixth position and swings out of the distal heme pocket. The flipping motion of the His81 imidazole group accompanies structural readjustments of some residues (Gln62, Phe63, Gln72, and Ser75) in both the CD‐corner and D‐helix regions of Cgb. On the other hand, no significant structural changes were observed in other Cgb regions, for example, on the proximal side. These structural alterations that occurred as a result of exogenous ligand (CO) binding are clearly different from those observed in other vertebrate hexa‐coordinated globins (mouse neuroglobin, Drosophila melanogaster hemoglobin) and penta‐coordinated sperm whale myoglobin. The present study provides the structural basis for further discussion of the unique ligand‐binding properties of Cgb. Proteins 2011. © 2011 Wiley‐Liss, Inc. |
format |
Article in Journal/Newspaper |
author |
Makino, Masatomo Sawai, Hitomi Shiro, Yoshitsugu Sugimoto, Hiroshi |
spellingShingle |
Makino, Masatomo Sawai, Hitomi Shiro, Yoshitsugu Sugimoto, Hiroshi Crystal structure of the carbon monoxide complex of human cytoglobin |
author_facet |
Makino, Masatomo Sawai, Hitomi Shiro, Yoshitsugu Sugimoto, Hiroshi |
author_sort |
Makino, Masatomo |
title |
Crystal structure of the carbon monoxide complex of human cytoglobin |
title_short |
Crystal structure of the carbon monoxide complex of human cytoglobin |
title_full |
Crystal structure of the carbon monoxide complex of human cytoglobin |
title_fullStr |
Crystal structure of the carbon monoxide complex of human cytoglobin |
title_full_unstemmed |
Crystal structure of the carbon monoxide complex of human cytoglobin |
title_sort |
crystal structure of the carbon monoxide complex of human cytoglobin |
publisher |
Wiley |
publishDate |
2011 |
url |
http://dx.doi.org/10.1002/prot.22950 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.22950 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.22950 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Proteins: Structure, Function, and Bioinformatics volume 79, issue 4, page 1143-1153 ISSN 0887-3585 1097-0134 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/prot.22950 |
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Proteins: Structure, Function, and Bioinformatics |
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79 |
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4 |
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1143 |
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1153 |
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1800738898851135488 |