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RESEARCH ARTICLE
Contents Vol 73(3)

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

Julian J. Adams A , Craig J. Morton https://orcid.org/0000-0001-5452-5193 B C and Michael W. Parker A B C
+ Author Affiliations
- Author Affiliations

A St Vincent’s Institute of Medical Research, 9 Princes Street, Fitzroy, Vic. 3065, Australia.

B Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 30 Flemington Road, Parkville, Vic. 3010, Australia.

C Corresponding authors. Email: Craig.Morton@unimelb.edu.au; mwp@unimelb.edu.au

Australian Journal of Chemistry 73(3) 145-150 https://doi.org/10.1071/CH19346
Submitted: 23 July 2019  Accepted: 26 August 2019   Published: 2 October 2019

Abstract

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.


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