6RUN

Co-substituted alpha-Keggin bound to Proteinase K solved by EP

6RUN の概要

• エントリーDOI: 10.2210/pdb6run/pdb
• 関連するPDBエントリー: 6RUG 6RUH 6RUK
• 分子名称: Proteinase K, Co-substituted alpha-Keggin, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: polyoxometalate, complex, alpha-keggin, proteinase k, protein binding
• 由来する生物種: Parengyodontium album
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34527.10

構造登録者

Breibeck, J.,Bijelic, A.,Rompel, A. (登録日: 2019-05-28, 公開日: 2019-09-18, 最終更新日: 2024-10-16)

主引用文献

Breibeck, J.,Bijelic, A.,Rompel, A.
Transition metal-substituted Keggin polyoxotungstates enabling covalent attachment to proteinase K upon co-crystallization.
Chem.Commun.(Camb.), 55:11519-11522, 2019

PubMed Abstract: The use of α- and β-Keggin polyoxotungstates (POTs) substituted by a single first row transition metal ion (CoII, NiII, CuII, ZnII) as superchaotropic crystallization additives led to covalent and non-covalent interactions with protein side-chains of proteinase K. Two major Keggin POT binding sites in proteinase K were identified, both stabilizing the orientation of the substituted metal site towards the protein surface and suggesting increased protein affinity for the substitution sites. The formation of all observed covalent bonds involves the same aspartate carboxylate, taking the role of a terminal oxygen with the Keggin α-isomer or even, in an unprecedented scenario, a bridging cluster oxygen with the β-isomer. Covalent bond formation with the protein carboxylate was observed only with the NiII- and CoII-substituted POTs, following the HSAB concept and the principle of metal immobilization.

PubMed: 31490500
DOI: 10.1039/c9cc05818d

実験手法

X-RAY DIFFRACTION (1.1 Å)