1XRE

Crystal Structure of SodA-2 (BA5696) from Bacillus anthracis at 1.8A Resolution.

1XRE の概要

• エントリーDOI: 10.2210/pdb1xre/pdb
• 分子名称: Superoxide dismutase, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: soda-2; superoxide dismutase; bacillus anthracis; ba5696; spine, oxidoreductase
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50329.56

構造登録者

Boucher, I.W.,Levdikov, V.M.,Blagova, E.V.,Fogg, M.J.,Brannigan, J.A.,Wilkinson, A.J.,Wilson, K.S. (登録日: 2004-10-14, 公開日: 2005-07-19, 最終更新日: 2023-08-23)

主引用文献

Boucher, I.W.,Kalliomaa, A.K.,Levdikov, V.M.,Blagova, E.V.,Fogg, M.J.,Brannigan, J.A.,Wilson, K.S.,Wilkinson, A.J.
Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre.
Acta Crystallogr.,Sect.F, 61:621-624, 2005

PubMed Abstract: The BA4499 and BA5696 genes of Bacillus anthracis encode proteins homologous to manganese superoxide dismutase, suggesting that this organism has an expanded repertoire of antioxidant proteins. Differences in metal specificity and quaternary structure between the dismutases of prokaryotes and higher eukaryotes may be exploited in the development of therapeutic antibacterial compounds. Here, the crystal structure of two Mn superoxide dismutases from B. anthracis solved to high resolution are reported. Comparison of their structures reveals that a highly conserved residue near the active centre is substituted in one of the proteins and that this is a characteristic feature of superoxide dismutases from the B. cereus/B. anthracis/B. thuringiensis group of organisms.

PubMed: 16511113
DOI: 10.1107/S1744309105017380

実験手法

X-RAY DIFFRACTION (1.8 Å)