6YH0

Marasmius oreades agglutinin (MOA) in complex with the truncated PVPRAHS synthetic substrate

This is a non-PDB format compatible entry.

Summary for 6YH0

• Entry DOI: 10.2210/pdb6yh0/pdb
• Related: 2IHO 3EF2 6TSL 6TSM
• Descriptor: Agglutinin, PRO-VAL-PRO-ARG, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose, ... (9 entities in total)
• Functional Keywords: fungal chimerolectin, papain-like cysteine protease, protease-substrate complex, calcium-binding protein, manganese-binding protein, toxin
• Biological source: Marasmius oreades; More
• Total number of polymer chains: 2
• Total formula weight: 34598.19

Authors

Cordara, G.,Manna, D.,Krengel, U. (deposition date: 2020-03-28, release date: 2020-07-29, Last modification date: 2024-10-23)

Primary citation

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

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: 34235469
DOI: 10.1016/j.crstbi.2020.04.003

Experimental method

X-RAY DIFFRACTION (1.56 Å)