3CEI

Crystal Structure of Superoxide Dismutase from Helicobacter pylori

3CEI の概要

• エントリーDOI: 10.2210/pdb3cei/pdb
• 分子名称: Superoxide dismutase, FE (III) ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Helicobacter pylori (Campylobacter pylori)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49303.08

構造登録者

Esposito, L.,Seydel, A.,Aiello, R.,Sorrentino, G.,Cendron, L.,Zanotti, G.,Zagari, A. (登録日: 2008-02-29, 公開日: 2008-06-10, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)