4KTU

Bovine trypsin in complex with microviridin J at pH 6.5

4KTU の概要

• エントリーDOI: 10.2210/pdb4ktu/pdb
• 関連するPDBエントリー: 3MYW 4KTS
• 関連するBIRD辞書のPRD_ID: PRD_001086
• 分子名称: Cationic trypsin, microviridin j, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: serine protease, hydrolase, natural product inhibitor, trypsin, protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Microcystis aeruginosa MRC; 詳細
• 細胞内の位置: Secreted, extracellular space: P00760
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25089.23

構造登録者

Quitterer, F.,Groll, M.,Hertweck, C.,Dittmann, E. (登録日: 2013-05-21, 公開日: 2014-04-02, 最終更新日: 2023-09-20)

主引用文献

Weiz, A.R.,Ishida, K.,Quitterer, F.,Meyer, S.,Kehr, J.C.,Muller, K.M.,Groll, M.,Hertweck, C.,Dittmann, E.
Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions.
Angew.Chem.Int.Ed.Engl., 53:3735-3738, 2014

PubMed Abstract: Understanding and controlling proteolysis is an important goal in therapeutic chemistry. Among the natural products specifically inhibiting proteases microviridins are particularly noteworthy. Microviridins are ribosomally produced and posttranslationally modified peptides that are processed into a unique, cagelike architecture. Here, we report a combined rational and random mutagenesis approach that provides fundamental insights into selectivity-conferring moieties of microviridins. The potent variant microviridin J was co-crystallized with trypsin, and for the first time the three-dimensional structure of microviridins was determined and the mode of inhibition revealed.

PubMed: 24591244
DOI: 10.1002/anie.201309721

実験手法

X-RAY DIFFRACTION (1.35 Å)