Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The three-dimensional structure of sperm whale myoglobin His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray crystallography at 1.6 A resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 A from the NH1 atom of Arg45(CD3), which is also pointing towards the distal site. Both are kept in this position by hydrogen bonding and electrostatic interactions with a solvent sulfate ion, located amongst the two, on the protein surface. No liganded water molecule is present at the sixth coordination position of the Fe(III) heme.
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.,Rizzi M, Bolognesi M, Coda A, Cutruzzola F, Allocatelli CT, Brancaccio A, Brunori M FEBS Lett. 1993 Mar 29;320(1):13-6. PMID:8462669[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rizzi M, Bolognesi M, Coda A, Cutruzzola F, Allocatelli CT, Brancaccio A, Brunori M. Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution. FEBS Lett. 1993 Mar 29;320(1):13-6. PMID:8462669
