1ESO

MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

1ESO の概要

• エントリーDOI: 10.2210/pdb1eso/pdb
• 分子名称: CU, ZN SUPEROXIDE DISMUTASE, ZINC ION, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, cu, zn superoxide dismutase, monomeric superoxide dismutase, copper enzymes, enzyme evolution, x-ray crystal structure
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P53635
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15889.54

構造登録者

Pesce, A.,Capasso, C.,Battistoni, A.,Folcarelli, S.,Rotilio, G.,Desideri, A.,Bolognesi, M. (登録日: 1997-06-27, 公開日: 1998-07-01, 最終更新日: 2024-11-06)

主引用文献

Pesce, A.,Capasso, C.,Battistoni, A.,Folcarelli, S.,Rotilio, G.,Desideri, A.,Bolognesi, M.
Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography.
J.Mol.Biol., 274:408-420, 1997

PubMed Abstract: The first three-dimensional structure of a functional monomeric Cu, Zn superoxide dismutase (from Escherichia coli, E_SOD) is reported at 2.0 A resolution (R-factor=16.8%). Compared to the homologous eukaryotic enzymes, E_SOD displays a perturbed antiparallel beta-barrel structure. The most striking structural features observed include extended amino acid insertions in the surface 1, 2-loop and S-S subloop, modification of the disulfide bridge connection, and loss of functional electrostatic residues, suggesting a modified control of substrate steering toward the catalytic center. The active site Cu2+ displays a distorted coordination sphere due to an unusually long bond to the metal-bridging residue His61. Inspection of the crystal packing does not show regions of extended contact indicative of a dimeric assembly. The molecular surface region involved in subunit dimerization in eukaryotic superoxide dismutases is structurally altered in E_SOD and displays a net polar nature.

PubMed: 9405149
DOI: 10.1006/jmbi.1997.1400

実験手法

X-RAY DIFFRACTION (2 Å)