8Y2U

Crystal structure of 3C protease from coxsackievirus B4

Summary for 8Y2U

• Entry DOI: 10.2210/pdb8y2u/pdb
• Descriptor: Protease 3C (2 entities in total)
• Functional Keywords: coxsackievirus b4, viral protein
• Biological source: Coxsackievirus B4
• Total number of polymer chains: 2
• Total formula weight: 40746.82

Authors

Jiang, H.H.,Lin, C.,Zhang, J.,Li, J. (deposition date: 2024-01-27, release date: 2024-08-14)

Primary citation

Jiang, H.,Lin, C.,Chang, J.,Zou, X.,Zhang, J.,Li, J.
Crystal structures of the 3C proteases from Coxsackievirus B3 and B4.
Acta Crystallogr.,Sect.F, 80:183-190, 2024

PubMed Abstract: Enteroviruses cause a wide range of disorders with varying presentations and severities, and some enteroviruses have emerged as serious public health concerns. These include Coxsackievirus B3 (CVB3), an active causative agent of viral myocarditis, and Coxsackievirus B4 (CVB4), which may accelerate the progression of type 1 diabetes. The 3C proteases from CVB3 and CVB4 play important roles in the propagation of these viruses. In this study, the 3C proteases from CVB3 and CVB4 were expressed in Escherichia coli and purified by affinity chromatography and gel-filtration chromatography. The crystals of the CVB3 and CVB4 3C proteases diffracted to 2.10 and 2.01 Å resolution, respectively. The crystal structures were solved by the molecular-replacement method and contained a typical chymotrypsin-like fold and a conserved His40-Glu71-Cys147 catalytic triad. Comparison with the structures of 3C proteases from other enteroviruses revealed high similarity with minor differences, which will guide the design of 3C-targeting inhibitors with broad-spectrum properties.

PubMed: 39052022
DOI: 10.1107/S2053230X24006915

Experimental method

X-RAY DIFFRACTION (2.01 Å)