2M5T

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

Summary for 2M5T

• Entry DOI: 10.2210/pdb2m5t/pdb
• NMR Information: BMRB: 19079
• Descriptor: human rhinovirus 2A proteinase, ZINC ION (2 entities in total)
• Functional Keywords: human rhinovirus c, 2a proteinase, cysteine proteinase, viral protein
• Biological source: Rhinovirus C
• Cellular location: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): I2CMJ2
• Total number of polymer chains: 1
• Total formula weight: 15617.70

Authors

Lee, W.,Frederick, R.,Tonelli, M.,Troupis, A.T.,Reinin, N.,Suchy, F.P.,Moyer, K.,Watters, K.,Aceti, D.,Palmenberg, A.C.,Markley, J.L. (deposition date: 2013-03-07, release date: 2014-03-19, Last modification date: 2024-05-15)

Primary citation

Lee, W.,Watters, K.E.,Troupis, A.T.,Reinen, N.M.,Suchy, F.P.,Moyer, K.L.,Frederick, R.O.,Tonelli, M.,Aceti, D.J.,Palmenberg, A.C.,Markley, J.L.
Solution Structure of the 2A Protease from a Common Cold Agent, Human Rhinovirus C2, Strain W12.
Plos One, 9:e97198-e97198, 2014

PubMed 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 Å 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.

PubMed: 24937088
DOI: 10.1371/journal.pone.0097198

Experimental method

SOLUTION NMR