Structural highlights
Function
[MYG_HORSE] 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
The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.
Three-dimensional structure of cyanomet-sulfmyoglobin C.,Evans SV, Sishta BP, Mauk AG, Brayer GD Proc Natl Acad Sci U S A. 1994 May 24;91(11):4723-6. PMID:8197124[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Evans SV, Sishta BP, Mauk AG, Brayer GD. Three-dimensional structure of cyanomet-sulfmyoglobin C. Proc Natl Acad Sci U S A. 1994 May 24;91(11):4723-6. PMID:8197124
