1HL5

The Structure of Holo Type Human Cu, Zn Superoxide Dismutase

1HL5 の概要

• エントリーDOI: 10.2210/pdb1hl5/pdb
• 関連するPDBエントリー: 1AZV 1BA9 1DSW 1FUN 1HL4 1KMG 1L3N 1MFM 1N18 1N19 1SOS 1SPD 4SOD
• 分子名称: SUPEROXIDE DISMUTASE, COPPER (II) ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, human cu, zn superoxide dismutase, antioxidant, metal-binding, amyotrophic lateral sclerosis, disease mutation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: P00441
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 287337.52

構造登録者

Strange, R.W.,Antonyuk, S.,Hough, M.A.,Doucette, P.,Rodriguez, J.,Hart, P.J.,Hayward, L.J.,Valentine, J.S.,Hasnain, S.S. (登録日: 2003-03-13, 公開日: 2003-05-08, 最終更新日: 2024-11-13)

主引用文献

Strange, R.W.,Antonyuk, S.,Hough, M.A.,Doucette, P.,Rodriguez, J.,Hart, P.J.,Hayward, L.J.,Valentine, J.S.,Hasnain, S.S.
The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis
J.Mol.Biol., 328:877-, 2003

PubMed Abstract: Cu, Zn superoxide dismutase (SOD1) forms a crucial component of the cellular defence against oxidative stress. Zn-deficient wild-type and mutant human SOD1 have been implicated in the disease familial amyotrophic lateral sclerosis (FALS). We present here the crystal structures of holo and metal-deficient (apo) wild-type protein at 1.8A resolution. The P21 wild-type holo enzyme structure has nine independently refined dimers and these combine to form a "trimer of dimers" packing motif in each asymmetric unit. There is no significant asymmetry between the monomers in these dimers, in contrast to the subunit structures of the FALS G37R mutant of human SOD1 and in bovine Cu,Zn SOD. Metal-deficient apo SOD1 crystallizes with two dimers in the asymmetric unit and shows changes in the metal-binding sites and disorder in the Zn binding and electrostatic loops of one dimer, which is devoid of metals. The second dimer lacks Cu but has approximately 20% occupancy of the Zn site and remains structurally similar to wild-type SOD1. The apo protein forms a continuous, extended arrangement of beta-barrels stacked up along the short crystallographic b-axis, while perpendicular to this axis, the constituent beta-strands form a zig-zag array of filaments, the overall arrangement of which has a similarity to the common structure associated with amyloid-like fibrils.

PubMed: 12729761
DOI: 10.1016/S0022-2836(03)00355-3

実験手法

X-RAY DIFFRACTION (1.8 Å)