The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin
We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)→Tyr; His(E7)→Gln; Thr(E10)→Arg] to 1.4-Å resolution by ultra-low temperature (20 K) x-ray diffraction. Starting with the CO complex, illumination leads to photolysis of the Fe–C...
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ftpubmed:oai:pubmedcentral.nih.gov:15753 2023-05-15T18:26:41+02:00 The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin Brunori, Maurizio Vallone, Beatrice Cutruzzolà, Francesca Travaglini-Allocatelli, Carlo Berendzen, Joel Chu, Kelvin Sweet, Robert M. Schlichting, Ilme 2000-02-29 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC15753 http://www.ncbi.nlm.nih.gov/pubmed/10681426 en eng The National Academy of Sciences http://www.ncbi.nlm.nih.gov/pmc/articles/PMC15753 http://www.ncbi.nlm.nih.gov/pubmed/10681426 Copyright © 2000, The National Academy of Sciences Biological Sciences Text 2000 ftpubmed 2013-08-29T06:46:01Z We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)→Tyr; His(E7)→Gln; Thr(E10)→Arg] to 1.4-Å resolution by ultra-low temperature (20 K) x-ray diffraction. Starting with the CO complex, illumination leads to photolysis of the Fe–CO bond, and migration of the photolyzed carbon monoxide (CO*) to a niche in the protein 8.1 Å from the heme iron; this cavity corresponds to that hosting an atom of Xe when the crystal is equilibrated with xenon gas at 7 atmospheres [Tilton, R. F., Jr., Kuntz, I. D. & Petsko, G. A. (1984) Biochemistry 23, 2849–2857]. The site occupied by CO* corresponds to that predicted by molecular dynamics simulations previously carried out to account for the NO geminate rebinding of Mb-YQR observed in laser photolysis experiments at room temperature. This secondary docking site differs from the primary docking site identified by previous crystallographic studies on the photolyzed intermediate of wild-type sperm whale Mb performed at cryogenic temperatures [Teng et al. (1994) Nat. Struct. Biol. 1, 701–705] and room temperature [Šrajer et al. (1996) Science 274, 1726–1729]. Our experiment shows that the pathway of a small molecule in its trajectory through a protein may be modified by site-directed mutagenesis, and that migration within the protein matrix to the active site involves a limited number of pre-existing cavities identified in the interior space of the protein. Text Sperm whale PubMed Central (PMC) |
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Biological Sciences Brunori, Maurizio Vallone, Beatrice Cutruzzolà, Francesca Travaglini-Allocatelli, Carlo Berendzen, Joel Chu, Kelvin Sweet, Robert M. Schlichting, Ilme The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin |
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Biological Sciences |
description |
We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)→Tyr; His(E7)→Gln; Thr(E10)→Arg] to 1.4-Å resolution by ultra-low temperature (20 K) x-ray diffraction. Starting with the CO complex, illumination leads to photolysis of the Fe–CO bond, and migration of the photolyzed carbon monoxide (CO*) to a niche in the protein 8.1 Å from the heme iron; this cavity corresponds to that hosting an atom of Xe when the crystal is equilibrated with xenon gas at 7 atmospheres [Tilton, R. F., Jr., Kuntz, I. D. & Petsko, G. A. (1984) Biochemistry 23, 2849–2857]. The site occupied by CO* corresponds to that predicted by molecular dynamics simulations previously carried out to account for the NO geminate rebinding of Mb-YQR observed in laser photolysis experiments at room temperature. This secondary docking site differs from the primary docking site identified by previous crystallographic studies on the photolyzed intermediate of wild-type sperm whale Mb performed at cryogenic temperatures [Teng et al. (1994) Nat. Struct. Biol. 1, 701–705] and room temperature [Šrajer et al. (1996) Science 274, 1726–1729]. Our experiment shows that the pathway of a small molecule in its trajectory through a protein may be modified by site-directed mutagenesis, and that migration within the protein matrix to the active site involves a limited number of pre-existing cavities identified in the interior space of the protein. |
format |
Text |
author |
Brunori, Maurizio Vallone, Beatrice Cutruzzolà, Francesca Travaglini-Allocatelli, Carlo Berendzen, Joel Chu, Kelvin Sweet, Robert M. Schlichting, Ilme |
author_facet |
Brunori, Maurizio Vallone, Beatrice Cutruzzolà, Francesca Travaglini-Allocatelli, Carlo Berendzen, Joel Chu, Kelvin Sweet, Robert M. Schlichting, Ilme |
author_sort |
Brunori, Maurizio |
title |
The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin |
title_short |
The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin |
title_full |
The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin |
title_fullStr |
The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin |
title_full_unstemmed |
The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin |
title_sort |
role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin |
publisher |
The National Academy of Sciences |
publishDate |
2000 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC15753 http://www.ncbi.nlm.nih.gov/pubmed/10681426 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC15753 http://www.ncbi.nlm.nih.gov/pubmed/10681426 |
op_rights |
Copyright © 2000, The National Academy of Sciences |
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1766208647636975616 |