1QKE

ERABUTOXIN

1QKE の概要

• エントリーDOI: 10.2210/pdb1qke/pdb
• 分子名称: ERABUTOXIN A, SULFATE ION (3 entities in total)
• 機能のキーワード: neurotoxin, erabutoxin
• 由来する生物種: Laticauda semifasciata (broad-banded blue sea krait)
• 細胞内の位置: Secreted : P60775
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6949.78

構造登録者

Nastopoulos, V.,Kanellopoulos, P.N.,Tsernoglou, D. (登録日: 1998-01-16, 公開日: 1999-02-16, 最終更新日: 2024-10-23)

主引用文献

Nastopoulos, V.,Kanellopoulos, P.N.,Tsernoglou, D.
Structure of dimeric and monomeric erabutoxin a refined at 1.5 A resolution.
Acta Crystallogr.,Sect.D, 54:964-974, 1998

PubMed Abstract: Erabutoxin a has been crystallized in its monomeric and dimeric forms. The structures were refined at 1.50 and 1.49 A resolution, respectively, using synchrotron radiation data. The crystals belong to space group P212121, with cell dimensions a = 49.84, b = 46.62, c = 21.22 A for the monomer and a = 55.32, b = 53.54, c = 40.76 A for the dimer. Using starting models from earlier structure determinations, the monomeric structure refined to an R value of 16.7% (8004 unique reflections, 17.0-1.50 A resolution range), while the dimeric structure has been solved by the molecular-replacement method with a final R value of 16.9% (19 444 unique reflections, 17.4-1.49 A resolution range). The high-resolution electron-density maps clearly revealed significant discrete disorder in the proteins and allowed an accurate determination of the solvent structure. For the monomer, the side chains of six residues were modelled with alternate conformers and 106 sites for water molecules and one site for a sulfate ion were included in the final model, whereas for the dimer, 206 sites for water molecules were included and both C-terminal residues together with the side chains of 11 residues adopted alternative conformations. A comparison was made with earlier structure determinations. The features of the solvent structure of the erabutoxin molecules are discussed in detail.

PubMed: 9757111
DOI: 10.1107/S0907444998005125

実験手法

X-RAY DIFFRACTION (1.5 Å)