Structural highlights
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 the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in ligand binding geometry. Oxygen binds to the heme iron in a bent conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two subunits. These observed angles are lower than the equivalent angles in the carbon monoxide-liganded form and intermediate between the angles observed in structures of oxygenated sperm whale myoglobin and oxygenated human hemoglobin. This third high resolution structure of Scapharca dimeric hemoglobin permits a detailed analysis of the water structure in the highly hydrated interface between subunits.
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution.,Condon PJ, Royer WE Jr J Biol Chem. 1994 Oct 14;269(41):25259-67. PMID:7929217[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Condon PJ, Royer WE Jr. Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution. J Biol Chem. 1994 Oct 14;269(41):25259-67. PMID:7929217
