1AJH
PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K
Summary for 1AJH
| Entry DOI | 10.2210/pdb1ajh/pdb |
| Descriptor | MYOGLOBIN, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | oxygen transport, respiratory protein, heme, photoproduct intermediate |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18071.57 |
| Authors | Teng, T.Y.,Srajer, V.,Moffat, K. (deposition date: 1997-05-02, release date: 1997-11-12, Last modification date: 2024-05-22) |
| Primary citation | Teng, T.Y.,Srajer, V.,Moffat, K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nat.Struct.Biol., 1:701-705, 1994 Cited by PubMed Abstract: Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins. PubMed: 7634074DOI: 10.1038/nsb1094-701 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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