5D62

MOA-Z-VAD-fmk complex, inverted orientation

Summary for 5D62

• Entry DOI: 10.2210/pdb5d62/pdb
• Related: 2IHO 3EF2 5D61
• Related PRD ID: PRD_000338
• Descriptor: Agglutinin, Z-VAD-fmk, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose, ... (10 entities in total)
• Functional Keywords: hydrolase, papain-like, protease, inhibitor, fungal
• Biological source: Marasmius oreades; More
• Total number of polymer chains: 2
• Total formula weight: 34795.49

Authors

Cordara, G.,Krengel, U. (deposition date: 2015-08-11, release date: 2016-03-02, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)