1NLI

Complex of [E160A-E189A] trichosanthin and adenine

1NLI の概要

• エントリーDOI: 10.2210/pdb1nli/pdb
• 分子名称: Ribosome-inactivating protein alpha-trichosanthin, ADENINE (3 entities in total)
• 機能のキーワード: protein-dna complex, ribosome-inactivating protein, hydrolase
• 由来する生物種: Trichosanthes kirilowii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27317.02

構造登録者

Shaw, P.C.,Wong, K.B.,Chan, D.S.B.,Williams, R.L. (登録日: 2003-01-07, 公開日: 2003-01-21, 最終更新日: 2023-08-16)

主引用文献

Shaw, P.C.,Wong, K.B.,Chan, D.S.,Williams, R.L.
Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine.
Toxicon, 41:575-581, 2003

PubMed Abstract: Trichosanthin is a ribosome-inactivating protein that cleaves specifically the N-glycosidic bond of A-4324 of 28S rRNA. Trichosanthin and its variant [E160A-E189A]-trichosanthin were found to bind an adenine base with a K(d) value of approximately 0.2mM. To determine how this doubly mutated variant of trichosanthin interacts with adenine, the co-crystal structure of [E160A-E189A]-trichosanthin and adenine was resolved to 0.193nm which revealed that the active site conformation of the doubly mutated variant is isomorphous to wild-type trichosanthin. Water molecules were found at locations corresponding to the eliminated side chain of Glu-160 and Glu-189. On the other hand, the adenine base interacted with [E160A-E189A]-trichosanthin in a manner similar to that in wild-type trichosanthin. Our structural analysis illustrates that Glu-160 and Glu-189 in trichosanthin do not play an important role in maintaining the active site conformation and binding adenine, an essential step for substrate-enzyme interaction. On the other hand, removal of two glutamate residues changed a large patch of negatively charged surface to a positive charge, which may account for the destabilization of the oxocarbenium-like transition-state and the significant decrease in ribosome-inactivating activity in [E160A-E189A]-trichosanthin.

PubMed: 12676436
DOI: 10.1016/S0041-0101(02)00387-2

実験手法

X-RAY DIFFRACTION (1.93 Å)