1D5N

CRYSTAL STRUCTURE OF E. COLI MNSOD AT 100K

1D5N の概要

• エントリーDOI: 10.2210/pdb1d5n/pdb
• 分子名称: PROTEIN (MANGANESE SUPEROXIDE DISMUTASE), MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: manganese superoxide dismutase, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 92207.26

構造登録者

Borgstahl, G.E.O.,Pokross, M.,Chehab, R.,Sekher, A.,Snell, E.H. (登録日: 1999-10-08, 公開日: 2000-03-02, 最終更新日: 2024-02-07)

主引用文献

Borgstahl, G.E.,Pokross, M.,Chehab, R.,Sekher, A.,Snell, E.H.
Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase.
J.Mol.Biol., 296:951-959, 2000

PubMed Abstract: Superoxide dismutase protects organisms from potentially damaging oxygen radicals by catalyzing the disproportionation of superoxide to oxygen and hydrogen peroxide. We report the use of cryogenic temperatures to kinetically capture the sixth ligand bound to the active site of manganese superoxide dismutase (MnSOD). Synchrotron X-ray diffraction data was collected from Escherichia coli MnSOD crystals grown at pH 8.5 and cryocooled to 100 K. Structural refinement to 1.55 A resolution and close inspection of the active site revealed electron density for a sixth ligand that was interpreted to be a hydroxide ligand. The six-coordinate, distorted-octahedral geometry assumed during inhibition by hydroxide is compared to the room temperature, five-coordinate, trigonal bipyramidal active site determined with crystals grown from practically identical conditions. The gateway residues Tyr34, His30 and a tightly bound water molecule are implicated in closing-off the active site and blocking the escape route of the sixth ligand.

PubMed: 10686094
DOI: 10.1006/jmbi.1999.3506

実験手法

X-RAY DIFFRACTION (1.55 Å)