Journal article

The Crystal Structure of the Manganese Superoxide Dismutase from Geobacillus stearothermophilus: Parker and Blake (1988) Revisited

Julian J Adams, Craig J Morton, Michael W Parker



Superoxide dismutase (SOD) is an almost ubiquitous metalloenzyme in aerobic organisms that catalyses the disproportionation of superoxide. Geobacillus stearothermophilus MnSOD is the only published MnSOD structure that does not have its coordinates publicly available, yet it is one of the more cited structures in the SOD literature. The structure has now been refined with modern programs, yielding a significantly improved structure which has been deposited in the Protein Data Bank. Importantly, the further refined structure reveals the presence of a catalytically important fifth ligand, water, to the metal centre, as observed in other SOD structures.


Funding Acknowledgements

The authors thank Jonathan Ridler of the University of Melbourne who was able to retrieve the MnSOD diffraction data from a 1988 eight track tape. J.J.A. acknowledges the contribution of former colleagues at Massey University, and in particular his Ph.D. supervisor Professor Geoff Jameson, for the analysis of tuning of the metal centre. M.W.P. is indebted to David Stuart who introduced him to the joys of protein refinement when both were at the University of Oxford. Funding from the Victorian Government Operational Infrastructure Support Scheme to St Vincent's Institute is acknowledged. M.W.P. is a National Health and Medical Research Council of Australia Research Fellow.