ISSN:
1432-1327
Keywords:
NMR
;
Superoxide dismutase
;
Solution structure
;
Monomeric mutants
;
Structure-function relationship
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
2 , has RMSD values with respect to the average structure of 0.94 ± 0.14 Å2 and 1.50 ± 0.14 Å2 for the backbone and the heavy atoms, respectively. The overall folding, which includes the classical eight-stranded Greek-key β-barrel and a short α-helix, is very close to that of the previously characterized monomeric mutant E133QM2SOD and to that of wild-type SOD. The region involved in the subunit-subunit interactions in the dimeric protein is confirmed to be disordered in the monomeric species. It is also observed that a sizable rearrangement of the charged groups of the electrostatic loop and of Arg143 takes place in the monomeric species. The width of the active site channel, both at its entrance and at the bottleneck of the active site, is discussed in the light of the influence on the enzymatic activity and the latter with respect to the overall charge. It is also confirmed that the NH proton of His63 shields the Cu(I) from the bulk solvent, thus supporting the suggestion that superoxide may interact with the reduced metal ion in an outer-sphere fashion.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s007750050353
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