1DO1
CARBONMONOXY-MYOGLOBIN MUTANT L29W AT 105K
Summary for 1DO1
| Entry DOI | 10.2210/pdb1do1/pdb |
| Related | 1DO1 1DO3 1DO4 1DO7 |
| Related PRD ID | PRD_900006 |
| Descriptor | MYOGLOBIN, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | heme, respiratory protein, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18645.14 |
| Authors | Ostermann, A.,Waschipky, R.,Parak, F.G.,Nienhaus, G.U. (deposition date: 1999-12-18, release date: 2000-01-05, Last modification date: 2024-11-06) |
| Primary citation | Ostermann, A.,Waschipky, R.,Parak, F.G.,Nienhaus, G.U. Ligand binding and conformational motions in myoglobin. Nature, 404:205-208, 2000 Cited by PubMed Abstract: Myoglobin, a small globular haem protein that binds gaseous ligands such as O2, CO and NO reversibly at the haem iron, serves as a model for studying structural and dynamic aspects of protein reactions. Time-resolved spectroscopic measurements after photodissociation of the ligand revealed a complex ligand-binding reaction with multiple kinetic intermediates, resulting from protein relaxation and movements of the ligand within the protein. To observe the structural changes induced by ligand dissociation, we have carried out X-ray crystallographic investigations of carbon monoxy-myoglobin (MbCO mutant L29W) crystals illuminated below and above 180 K, complemented by time-resolved infrared spectroscopy of CO rebinding. Here we show that below 180 K photodissociated ligands migrate to specific sites within an internal cavity--the distal haem pocket--of an essentially immobilized, frozen protein, from where they subsequently rebind by thermally activated barrier crossing. Upon photodissociation above 180 K, ligands escape from the distal pocket, aided by protein fluctuations that transiently open exit channels. We recover most of the ligands in a cavity on the opposite side of the haem group. PubMed: 10724176DOI: 10.1038/35004622 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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