3ERA

RECOMBINANT ERABUTOXIN A (S8T MUTANT)

3ERA の概要

• エントリーDOI: 10.2210/pdb3era/pdb
• 分子名称: ERABUTOXIN A, THIOCYANATE ION (3 entities in total)
• 機能のキーワード: snake neurotoxin, venom, postsynaptic neurotoxin, neurotoxin
• 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: 2
• 化学式量合計: 13909.73

構造登録者

Gaucher, J.F.,Menez, R.,Arnoux, B.,Menez, A.,Ducruix, A. (登録日: 1997-06-25, 公開日: 1997-12-31, 最終更新日: 2024-04-03)

主引用文献

Gaucher, J.F.,Menez, R.,Arnoux, B.,Menez, A.,Ducruix, A.
High resolution x-ray analysis of two mutants of a curaremimetic snake toxin
Eur.J.Biochem., 267:1323-1329, 2000

PubMed Abstract: A previous mutational analysis of erabutoxin a (Ea), a curaremimetic toxin from sea snake venom, showed that the substitutions S8G and S8T caused, respectively, 176-fold and 780-fold affinity decreases for the nicotinic acetylcholine receptor (AchR). In view of the fact that the side-chain of Ser8 is buried in the wild-type toxin, we wondered whether these affinity changes reflect a direct binding contribution of S8 to the receptor and/or conformational changes that could have occurred in Ea as a result of the introduced mutations. To approach this question, we solved X-ray structures of the two mutants S8G and S8T at high resolution (0.18 nm and 0.17 nm, with R factors of 18.0% and 17.9%, respectively). The data show that none of the mutations significantly modified the toxin structure. Even within the site where the toxin binds to the receptor the backbone conformation remained unchanged. Therefore, the low affinities of the mutants S8T and S8G cannot be explained by a large conformational change of the toxin structure. Although we cannot exclude the possibility that undetectable structural changes have occurred in the toxin mutants, our data support the view that, although buried between loop I and II, S8 is part of the functional epitope of the toxin.

PubMed: 10691969
DOI: 10.1046/j.1432-1327.2000.01099.x

実験手法

X-RAY DIFFRACTION (1.7 Å)