5D63

MOA-Z-VAD-fmk inhibitor complex, direct/inverted dual orientation

5D63 の概要

• エントリーDOI: 10.2210/pdb5d63/pdb
• 関連するPDBエントリー: 2IHO 3EF2 5D61 5D62
• 関連するBIRD辞書のPRD_ID: PRD_000338
• 分子名称: Agglutinin, Z-VAD-fmk, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose, ... (10 entities in total)
• 機能のキーワード: hydrolase, papain-like, inhibitor, protease, fungal
• 由来する生物種: Marasmius oreades; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34817.90

構造登録者

Cordara, G.,Krengel, U. (登録日: 2015-08-11, 公開日: 2016-03-02, 最終更新日: 2024-11-20)

主引用文献

Cordara, G.,van Eerde, A.,Grahn, E.M.,Winter, H.C.,Goldstein, I.J.,Krengel, U.
An Unusual Member of the Papain Superfamily: Mapping the Catalytic Cleft of the Marasmius oreades agglutinin (MOA) with a Caspase Inhibitor.
Plos One, 11:e0149407-e0149407, 2016

PubMed Abstract: Papain-like cysteine proteases (PLCPs) constitute the largest group of thiol-based protein degrading enzymes and are characterized by a highly conserved fold. They are found in bacteria, viruses, plants and animals and involved in a number of physiological and pathological processes, parasitic infections and host defense, making them interesting targets for drug design. The Marasmius oreades agglutinin (MOA) is a blood group B-specific fungal chimerolectin with calcium-dependent proteolytic activity. The proteolytic domain of MOA presents a unique structural arrangement, yet mimicking the main structural elements in known PLCPs. Here we present the X-ray crystal structure of MOA in complex with Z-VAD-fmk, an irreversible caspase inhibitor known to cross-react with PLCPs. The structural data allow modeling of the substrate binding geometry and mapping of the fundamental enzyme-substrate interactions. The new information consolidates MOA as a new, yet strongly atypical member of the papain superfamily. The reported complex is the first published structure of a PLCP in complex with the well characterized caspase inhibitor Z-VAD-fmk.

PubMed: 26901797
DOI: 10.1371/journal.pone.0149407

実験手法

X-RAY DIFFRACTION (1.65 Å)