1ABS
PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K
Summary for 1ABS
| Entry DOI | 10.2210/pdb1abs/pdb |
| Descriptor | MYOGLOBIN, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | oxygen storage, intermediate in ligand binding, respiratory protein |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18105.72 |
| Authors | Schlichting, I.,Berendzen, J.,Phillips Jr., G.N.,Sweet, R.M. (deposition date: 1997-01-28, release date: 1997-04-01, Last modification date: 2024-05-22) |
| Primary citation | Schlichting, I.,Berendzen, J.,Phillips Jr., G.N.,Sweet, R.M. Crystal structure of photolysed carbonmonoxy-myoglobin. Nature, 371:808-812, 1994 Cited by PubMed Abstract: Myoglobin is a globular haem protein that reversibly binds ligands such as O2 and CO. Single photons of visible light can break the covalent bond between CO and the haem iron in carbon-monoxy-myoglobin (MbCO) and thus form an unstable intermediate, Mb*CO, with the CO inside the protein. The ensuing rebinding process has been extensively studied as a model for the interplay of dynamics, structure and function in protein reactions. We have used X-ray crystallography at liquid-helium temperatures to determine the structure of Mb*CO to a resolution of 1.5 A. The photodissociated CO lies on top of the haem pyrrole ring C. Comparison with the CO-bound and unligated myoglobin structures reveals that on photodissociation of the CO, the haem 'domes', the iron moves partially out of the haem plane, the iron-proximal histidine bonds is compressed, the F helix is strained and the distal histidine swings towards the outside of the ligand-binding pocket. PubMed: 7935843DOI: 10.1038/371808a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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