7EOX

Protease structure from Euphorbia resinifera

Summary for 7EOX

• Entry DOI: 10.2210/pdb7eox/pdb
• Descriptor: Protease, beta-D-xylopyranose-(1-2)-[alpha-D-mannopyranose-(1-3)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: euphorbia resinifera, plant latex, serine protease, plant protein
• Biological source: Euphorbia resinifera
• Total number of polymer chains: 2
• Total formula weight: 140372.57

Authors

Siritapetawee, J.,Attarataya, J.,Charoenwattanasatien, R. (deposition date: 2021-04-24, release date: 2022-01-12, Last modification date: 2024-10-23)

Primary citation

Siritapetawee, J.,Attarataya, J.,Charoenwattanasatien, R.
Sequence analysis and crystal structure of a glycosylated protease from Euphorbia resinifera latex for its proteolytic activity aspect.
Biotechnol Appl Biochem, 69:2580-2591, 2022

PubMed Abstract: The investigation of a plant glycosylated serine protease (EuRP-61) isolated from Euphorbia resinifera latex for potential antiplatelet and anticoagulation activities has been previously reported. In the present study, the protein sequence and native crystal structure of EuRP-61 were characterized. The structure was identified using single-wavelength anomalous diffraction with a refinement resolution of 1.7 Å (PDB ID: 7EOX). The main structural components of EuRP-61 were composed of three domains: catalytic, protease-associated (PA), and fibronectin type III (Fn3)-like domains. The crystal structure revealed that some loops in the PA and catalytic domains of EuRP-61 were different from the other subtilisin-like proteases (cucumisin and SBT3). These different loops might be involved in the general monomer formation of EuRP-61, substrate specificity, and maintenance of the catalytic domain. The Fn3-like domain may provide flexibility to the enzyme to bind with various substrates and cell receptors. Additionally, the active site of EuRP-61 consisted of the catalytic triad of Ser434, His106, and Asp32, similar to other serine proteases. The present study provides additional information and insight into the protease and antithrombotic activities of EuRP-61, which could contribute to further development of this enzyme for biomedical treatment.

PubMed: 34967474
DOI: 10.1002/bab.2307

Experimental method

X-RAY DIFFRACTION (1.7 Å)