Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution
The crystal structure of the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in l...
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ftunivmassmm:oai:repository.escholarship.umassmed.edu:20.500.14038/42471 2023-05-15T18:26:43+02:00 Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution Condon, Peter J. Royer, William E. Department of Biochemistry and Molecular Pharmacology Program in Molecular Medicine 2022-08-11T08:10:04.000 https://hdl.handle.net/20.500.14038/42471 https://escholarship.umassmed.edu/oapubs/817 en_US eng Link to Article in PubMed http://www.jbc.org/content/269/41/25259.long J Biol Chem. 1994 Oct 14;269(41):25259-67. 0021-9258 (Print) 7929217 http://hdl.handle.net/20.500.14038/42471 https://escholarship.umassmed.edu/oapubs/817 579703 oapubs/817 The Journal of biological chemistry 269 41 25259-67 Animals Binding Sites Bivalvia Computer Simulation Crystallography X-Ray Heme Hemoglobins Ligands Models Molecular Oxyhemoglobins Protein Conformation Water Life Sciences Medicine and Health Sciences Journal Article 2022 ftunivmassmm https://doi.org/20.500.14038/42471 2023-01-05T18:38:09Z The crystal structure of the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in ligand binding geometry. Oxygen binds to the heme iron in a bent conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two subunits. These observed angles are lower than the equivalent angles in the carbon monoxide-liganded form and intermediate between the angles observed in structures of oxygenated sperm whale myoglobin and oxygenated human hemoglobin. This third high resolution structure of Scapharca dimeric hemoglobin permits a detailed analysis of the water structure in the highly hydrated interface between subunits. Article in Journal/Newspaper Sperm whale University of Massachusetts, Medical School: eScholarship@UMMS |
institution |
Open Polar |
collection |
University of Massachusetts, Medical School: eScholarship@UMMS |
op_collection_id |
ftunivmassmm |
language |
English |
topic |
Animals Binding Sites Bivalvia Computer Simulation Crystallography X-Ray Heme Hemoglobins Ligands Models Molecular Oxyhemoglobins Protein Conformation Water Life Sciences Medicine and Health Sciences |
spellingShingle |
Animals Binding Sites Bivalvia Computer Simulation Crystallography X-Ray Heme Hemoglobins Ligands Models Molecular Oxyhemoglobins Protein Conformation Water Life Sciences Medicine and Health Sciences Condon, Peter J. Royer, William E. Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution |
topic_facet |
Animals Binding Sites Bivalvia Computer Simulation Crystallography X-Ray Heme Hemoglobins Ligands Models Molecular Oxyhemoglobins Protein Conformation Water Life Sciences Medicine and Health Sciences |
description |
The crystal structure of the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in ligand binding geometry. Oxygen binds to the heme iron in a bent conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two subunits. These observed angles are lower than the equivalent angles in the carbon monoxide-liganded form and intermediate between the angles observed in structures of oxygenated sperm whale myoglobin and oxygenated human hemoglobin. This third high resolution structure of Scapharca dimeric hemoglobin permits a detailed analysis of the water structure in the highly hydrated interface between subunits. |
author2 |
Department of Biochemistry and Molecular Pharmacology Program in Molecular Medicine |
format |
Article in Journal/Newspaper |
author |
Condon, Peter J. Royer, William E. |
author_facet |
Condon, Peter J. Royer, William E. |
author_sort |
Condon, Peter J. |
title |
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution |
title_short |
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution |
title_full |
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution |
title_fullStr |
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution |
title_full_unstemmed |
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution |
title_sort |
crystal structure of oxygenated scapharca dimeric hemoglobin at 1.7-a resolution |
publishDate |
2022 |
url |
https://hdl.handle.net/20.500.14038/42471 https://escholarship.umassmed.edu/oapubs/817 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
The Journal of biological chemistry 269 41 25259-67 |
op_relation |
Link to Article in PubMed http://www.jbc.org/content/269/41/25259.long J Biol Chem. 1994 Oct 14;269(41):25259-67. 0021-9258 (Print) 7929217 http://hdl.handle.net/20.500.14038/42471 https://escholarship.umassmed.edu/oapubs/817 579703 oapubs/817 |
op_doi |
https://doi.org/20.500.14038/42471 |
_version_ |
1766208695081893888 |