3cei
From Proteopedia
Crystal Structure of Superoxide Dismutase from Helicobacter pylori
Structural highlights
FunctionSODF_HELPY Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSuperoxide 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. The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension.,Esposito L, Seydel A, Aiello R, Sorrentino G, Cendron L, Zanotti G, Zagari A Biochim Biophys Acta. 2008 Nov;1784(11):1601-6. Epub 2008 May 6. PMID:18502213[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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