Structural highlights
Function
[MYG_THUAL] 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 crystal structure of metmyoglobin from yellowfin tuna (Thunnus albacares) has been determined by molecular replacement methods and refined to a conventional R factor of 0.177 for all observed reflections in the range of 6.0-1.70 A resolution. Like other myoglobins for which a high-resolution structure is available, the polypeptide chain is organized into several helices that cooperate to form a hydrophobic pocket into which the heme prosthetic group is non-covalently bound; however, the D helix observed in other myoglobins is absent in myoglobin from yellowfin tuna and has been replaced with a random coil. As well, the A helix has a pronounced kink due to the presence of Pro16. The differences in structure between this and sperm whale myoglobin can be correlated with their reported dioxygen affinity and dissociation. The structure is in agreement with reported fluorescence data which show an increased Trp14.heme distance in yellowfin tuna compared to sperm whale myoglobin.
1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix.,Birnbaum GI, Evans SV, Przybylska M, Rose DR Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):283-9. PMID:15299440[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Birnbaum GI, Evans SV, Przybylska M, Rose DR. 1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix. Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):283-9. PMID:15299440 doi:10.1107/S0907444993014271
