4YET

X-ray crystal structure of superoxide dismutase from Babesia bovis solved by Sulfur SAD

「4K2W」から置き換えられました

4YET の概要

• エントリーDOI: 10.2210/pdb4yet/pdb
• 関連するPDBエントリー: 4K2W
• 分子名称: Superoxide dismutase, FE (III) ION (3 entities in total)
• 機能のキーワード: superoxide dismutase, ssgcid, structural genomics, seattle structural genomics center for infectious disease, oxidoreductase
• 由来する生物種: Babesia bovis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45915.31

構造登録者

Fairman, J.W.,Clifton, M.C.,Abendroth, J.,Edwards, T.E.,Lorimer, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2015-02-24, 公開日: 2015-04-15, 最終更新日: 2024-02-28)

主引用文献

Phan, I.Q.,Davies, D.R.,Moretti, N.S.,Shanmugam, D.,Cestari, I.,Anupama, A.,Fairman, J.W.,Edwards, T.E.,Stuart, K.,Schenkman, S.,Myler, P.J.
Iron superoxide dismutases in eukaryotic pathogens: new insights from Apicomplexa and Trypanosoma structures.
Acta Crystallogr.,Sect.F, 71:615-621, 2015

PubMed Abstract: Prior studies have highlighted the potential of superoxide dismutases as drug targets in eukaryotic pathogens. This report presents the structures of three iron-dependent superoxide dismutases (FeSODs) from Trypanosoma cruzi, Leishmania major and Babesia bovis. Comparison with existing structures from Plasmodium and other trypanosome isoforms shows a very conserved overall fold with subtle differences. In particular, structural data suggest that B. bovis FeSOD may display similar resistance to peroxynitrite-mediated inactivation via an intramolecular electron-transfer pathway as previously described in T. cruzi FeSOD isoform B, thus providing valuable information for structure-based drug design. Furthermore, lysine-acetylation results in T. cruzi indicate that acetylation occurs at a position close to that responsible for the regulation of acetylation-mediated activity in the human enzyme.

PubMed: 25961325
DOI: 10.1107/S2053230X15004185

実験手法

X-RAY DIFFRACTION (1.75 Å)