2hhd: Difference between revisions

==Overview==

The crystal structure of the mutant deoxyhemoglobin in which the, beta-globin Val67(E11) has been replaced with threonine [Fronticelli et, al. (1993) Biochemistry 32, 1235-1242] has been determined at 2.2 A, resolution. Prior to the crystal structure determination, molecular, modeling indicated that the Thr67(E11) side chain hydroxyl group in the, distal beta-heme pocket forms a hydrogen bond with the backbone carbonyl, of His63(E7) and is within hydrogen-bonding distance of the N delta of, His63(E7). The mutant crystal structure indicates only small changes in, conformation in the vicinity of the E11 mutation confirming the molecular, modeling predictions. Comparison of the structures of the mutant, beta-subunits and recombinant porcine myoglobin with the identical, mutation [Cameron et al. (1993) Biochemistry 32, 13061-13070] indicates, similar conformations of residues in the distal heme pocket, but there is, no water molecule associated with either of the threonines of the, beta-subunits. The introduction of threonine into the distal heme pocket, despite having only small perturbations in the local structure, has a, marked affect on the interaction with ligands. In the oxy derivative there, is a 2-fold decrease in O2 affinity [Fronticelli et al. (1993), Biochemistry 32, 1235-1242], and the rate of autoxidation is increased by, 2 orders of magnitude. In the CO derivative the IR spectrum shows, modifications with respect to that of normal human hemoglobin, suggesting, the presence of multiple CO conformers. In the nitrosyl derivative an, interaction with the O gamma atom of Thr67(E11) is probably responsible, for the 10-fold increase in the rate of NO release from the beta-subunits., In the aquomet derivative there is a 6-fold decrease in the rate of hemin, dissociation suggesting an interaction of the Fe-coordinated water with, the O gamma of Thr67(E11).

==About this Structure==

[[Category: oxygen transport]]