4XFQ

Crystal Structure Basis for PEDV 3C Like Protease

Summary for 4XFQ

• Entry DOI: 10.2210/pdb4xfq/pdb
• Descriptor: PEDV main protease (2 entities in total)
• Functional Keywords: porcine epidemic diarrhea virus, 3c-like protease, hydrolase
• Biological source: Porcine epidemic diarrhea virus
• Cellular location: Host cytoplasm . Host cytoplasm, host perinuclear region . Host membrane ; Multi-pass membrane protein : K4L9I6
• Total number of polymer chains: 2
• Total formula weight: 66591.28

Authors

Ye, G.,Fu, Z.F.,Peng, G.Q. (deposition date: 2014-12-28, release date: 2016-01-20, Last modification date: 2023-11-08)

Primary citation

Ye, G.,Deng, F.,Shen, Z.,Luo, R.,Zhao, L.,Xiao, S.,Fu, Z.F.,Peng, G.
Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease.
Virology, 494:225-235, 2016

PubMed Abstract: Porcine epidemic diarrhea virus (PEDV), a member of the genus Alphacoronavirus, has caused significant damage to the Asian and American pork industries. Coronavirus 3C-like protease (3CL(pro)), which is involved in the processing of viral polyproteins for viral replication, is an appealing antiviral drug target. Here, we present the crystal structures of PEDV 3CL(pro) and a molecular complex between an inactive PEDV 3CL(pro) variant C144A bound to a peptide substrate. Structural characterization, mutagenesis and biochemical analysis reveal the substrate-binding pockets and the residues that comprise the active site of PEDV 3CL(pro). The dimerization of PEDV 3CL(pro) is similar to that of other Alphacoronavirus 3CL(pro)s but has several differences from that of SARS-CoV 3CL(pro) from the genus Betacoronavirus. Furthermore, the non-conserved motifs in the pockets cause different cleavage of substrate between PEDV and SARS-CoV 3CL(pro)s, which may provide new insights into the recognition of substrates by 3CL(pro)s in various coronavirus genera.

PubMed: 27128350
DOI: 10.1016/j.virol.2016.04.018

Experimental method

X-RAY DIFFRACTION (1.65 Å)