Structural highlights
Function
[MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of photolysed carbonmonoxy-myoglobin.,Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM Nature. 1994 Oct 27;371(6500):808-12. PMID:7935843[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM. Crystal structure of photolysed carbonmonoxy-myoglobin. Nature. 1994 Oct 27;371(6500):808-12. PMID:7935843 doi:http://dx.doi.org/10.1038/371808a07969399
