5D5R
Horse-heart myoglobin - deoxy state
Summary for 5D5R
| Entry DOI | 10.2210/pdb5d5r/pdb |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | myoglobin, heme protein, oxygen storage |
| Biological source | Equus caballus (Horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 17542.95 |
| Authors | Barends, T.,Schlichting, I. (deposition date: 2015-08-11, release date: 2015-09-16, Last modification date: 2024-01-10) |
| Primary citation | Barends, T.R.,Foucar, L.,Ardevol, A.,Nass, K.,Aquila, A.,Botha, S.,Doak, R.B.,Falahati, K.,Hartmann, E.,Hilpert, M.,Heinz, M.,Hoffmann, M.C.,Kofinger, J.,Koglin, J.E.,Kovacsova, G.,Liang, M.,Milathianaki, D.,Lemke, H.T.,Reinstein, J.,Roome, C.M.,Shoeman, R.L.,Williams, G.J.,Burghardt, I.,Hummer, G.,Boutet, S.,Schlichting, I. Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation. Science, 350:445-450, 2015 Cited by PubMed Abstract: The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein. PubMed: 26359336DOI: 10.1126/science.aac5492 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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