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Updated: Jul 5, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension
Luciana Esposito1, Anke Seydel, Rosa Aiello
1Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134, Naples, Italy. luciana.esposito@unina.it
Abstract:
Superoxide dismutases (SODs) are key enzymes for fighting oxidative stress. Helicobacter pylori produces a single SOD (HpSOD) which contains iron. The structure of this antioxidant protein has been determined at 2.4 A resolution. It is a dimer of two identical subunits with one iron ion per monomer. The protein shares 53% sequence identity with the corresponding enzyme from Escherichia coli. The model is compared with those of other dimeric Fe-containing SODs. HpSOD shows significant differences in relation to other SODs, the most important being an extended C-terminal tail. This structure provides a model for closely related sequences from species such as Campylobacter, where no structures are currently known. The structure of extended carboxyl termini is discussed in light of putative functions it may serve.
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