2M5T: Solution structure of the 2A proteinase from a common cold agent, human rhinovirus RV-C02, strain W12

Citation:
Abstract
Human rhinovirus strains differ greatly in their virulence, and this has been correlated with the differing substrate specificity of the respective 2A protease (2Apro). Rhinoviruses use their 2Apro to cleave a spectrum of cellular proteins important to virus replication and anti-host activities. These enzymes share a chymotrypsin-like fold stabilized by a tetra-coordinated zinc ion. The catalytic triad consists of conserved Cys (C105), His (H34), and Asp (D18) residues. We used a semi-automated NMR protocol developed at NMRFAM to determine the solution structure of 2Apro (C105A variant) from an isolate of the clinically important rhinovirus C species (RV-C). The backbone of C2 2Apro superimposed closely (1.41-1.81 A rmsd) with those of orthologs from RV-A2, coxsackie B4 (CB4), and enterovirus 71 (EV71) having sequence identities between 40% and 60%. Comparison of the structures suggest that the differential functional properties of C2 2Apro stem from its unique surface charge, high proportion of surface aromatics, and sequence surrounding the di-tyrosine flap.
PDB ID: 2M5TDownload
MMDB ID: 118329
PDB Deposition Date: 2013/3/7
Updated in MMDB: 2014/07
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2M5T: monomeric; determined by author
Molecular Components in 2M5T
Label Count Molecule
Protein (1 molecule)
1
Human Rhinovirus 2A Proteinase
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
Molecule information is not avaliable.
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