5MU9

MOA-E-64 complex

5MU9 の概要

• エントリーDOI: 10.2210/pdb5mu9/pdb
• 関連するPDBエントリー: 2IHO 3EF2 5D61 5D62 5D63
• 分子名称: Agglutinin, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]alpha-D-galactopyranose, ... (9 entities in total)
• 機能のキーワード: papain-like protease, e-64 inhibitor complex, lectin, calcium-binding, sugar binding protein
• 由来する生物種: Marasmius oreades
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34386.72

構造登録者

Cordara, G.,Manna, D.,Krengel, U. (登録日: 2017-01-12, 公開日: 2017-07-12, 最終更新日: 2024-11-06)

主引用文献

Cordara, G.,Manna, D.,Krengel, U.
Family of Papain-Like Fungal Chimerolectins with Distinct Ca(2+)-Dependent Activation Mechanism.
Biochemistry, 56:4689-4700, 2017

PubMed Abstract: An important function of fungal lectins is to protect their host. Marasmius oreades agglutinin (MOA) is toxic to nematodes and exerts its protective effect through protease activity. Its proteolytic function is associated with a papain-like dimerization domain. The closest homologue of MOA is Polyporus squamosus lectin 1a (PSL1a). Here, we probed PSL1a for catalytic activity and confirmed that it is a calcium-dependent cysteine protease, like MOA. The X-ray crystal structures of PSL1a (1.5 Å) and MOA (1.3 Å) in complex with calcium and the irreversible cysteine protease inhibitor E-64 elucidated the structural basis for their mechanism of action. The comparison with other calcium-dependent proteases (calpains, LapG) reveals a unique metal-dependent activation mechanism relying on a calcium-induced backbone shift and intradimer cooperation. Intriguingly, the enzymes appear to use a tyrosine-gating mechanism instead of pro-peptide processing. A search for potential MOA orthologues suggests the existence of a whole new family of fungal chimerolectins with these unique features.

PubMed: 28665586
DOI: 10.1021/acs.biochem.7b00317

実験手法

X-RAY DIFFRACTION (1.3 Å)