6TSO の概要
| エントリーDOI | 10.2210/pdb6tso/pdb |
| 関連するPDBエントリー | 2IHO 3EF2 6TSP |
| 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, ... (8 entities in total) |
| 機能のキーワード | fungal chimerolectin, papain-like cysteine protease, protease-substrate complex, calcium-binding protein, manganese-binding protein, toxin, 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 | 34184.06 |
| 構造登録者 | |
| 主引用文献 | Manna, D.,Cordara, G.,Krengel, U. Crystal structure of MOA in complex with a peptide fragment: A protease caught in flagranti . Curr Res Struct Biol, 2:56-67, 2020 Cited by PubMed Abstract: The agglutinin (MOA) is the holotype of an emerging family of fungal chimerolectins and an active Ca/Mn-dependent protease, which exhibits a unique papain-like fold with special active site features. Here we investigated the functional significance of the structural elements differentiating MOA from other papain-like cysteine proteases. X-ray crystal structures of MOA co-crystallized with two synthetic substrates reveal cleaved peptides bound to the catalytic site, corresponding to the final products of the proteolytic reaction. Anomalous diffraction data on crystals grown in the presence of calcium and manganese, cadmium or zinc resolve the calcium/manganese preference of MOA and elucidate the inhibitory roles of zinc and cadmium towards papain-like cysteine proteases in general. The reported structures, together with activity data of MOA active site variants, point to a conservation of the general proteolysis mechanism established for papain. Ultimately, the findings suggest that papain and the papain-like domain of MOA are the product of convergent evolution. PubMed: 34235469DOI: 10.1016/j.crstbi.2020.04.003 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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