3CEI

Crystal Structure of Superoxide Dismutase from Helicobacter pylori

Summary for 3CEI

• Entry DOI: 10.2210/pdb3cei/pdb
• Descriptor: Superoxide dismutase, FE (III) ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Helicobacter pylori (Campylobacter pylori)
• Total number of polymer chains: 2
• Total formula weight: 49303.08

Authors

Esposito, L.,Seydel, A.,Aiello, R.,Sorrentino, G.,Cendron, L.,Zanotti, G.,Zagari, A. (deposition date: 2008-02-29, release date: 2008-06-10, Last modification date: 2023-11-01)

Primary citation

Esposito, L.,Seydel, A.,Aiello, R.,Sorrentino, G.,Cendron, L.,Zanotti, G.,Zagari, A.
The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension
Biochim.Biophys.Acta, 1784:1601-1606, 2008

PubMed 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.

PubMed: 18502213
DOI: 10.1016/j.bbapap.2008.04.024

Experimental method

X-RAY DIFFRACTION (2.4 Å)