5EBX

THE CRYSTAL STRUCTURE OF ERABUTOXIN A AT 2.0 ANGSTROMS RESOLUTION

5EBX の概要

• エントリーDOI: 10.2210/pdb5ebx/pdb
• 関連するPDBエントリー: 3EBX
• 分子名称: ERABUTOXIN A, SULFATE ION (3 entities in total)
• 機能のキーワード: toxin
• 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

Corfield, P.W.R.,Lee, T.-J.,Low, B.W. (登録日: 1989-12-20, 公開日: 1990-04-15, 最終更新日: 2024-11-20)

主引用文献

Corfield, P.W.,Lee, T.J.,Low, B.W.
The crystal structure of erabutoxin a at 2.0-A resolution.
J.Biol.Chem., 264:9239-9242, 1989

PubMed Abstract: The three-dimensional structure of erabutoxin a, a single-chain, 62-residue protein neurotoxin from snake venom, has been determined to 2.0-A resolution by x-ray crystal structure analysis. Molecular replacement methods were used, and the structure refined to a residual R = 0.17. The sites of 62 water molecules and 1 sulfate ion have been located and refined. The structure of erabutoxin a is very similar to that established earlier for erabutoxin b. These toxins from venom of the same snake differ in sequence only at residue 26, which is Asn in erabutoxin a and His in erabutoxin b. The substitution leads to only minor variations in intramolecular hydrogen bonding. Furthermore, the distribution of thermal parameters and the implied regional mobilities are similar in the two structures. In particular, the highly mobile character of the peripheral segment Pro44-Gly49 in both structures supports the specific role proposed for this segment in neurotoxin binding to the acetylcholine receptor. Forty-eight of the solvent sites determined are first surface positions; approximately one-half of these are equivalent to solvent sites in erabutoxin b.

PubMed: 2722828

実験手法

X-RAY DIFFRACTION (2 Å)