3TN9

X-ray structure of the HRV2 empty capsid (B-particle)

Summary for 3TN9

• Entry DOI: 10.2210/pdb3tn9/pdb
• Related: 1FPN
• Descriptor: Protein VP1, Protein VP2, Protein VP3 (3 entities in total)
• Functional Keywords: empty capsid, b-particle, 80s particle, rhinovirus, hrv2, uncoating, rossmann fold, virus
• Biological source: Human rhinovirus 2 (HRV-2); More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P04936 P04936 P04936
• Total number of polymer chains: 3
• Total formula weight: 88042.18

Authors

Garriga, D.,Pickl-Herk, A.,Luque, D.,Wruss, J.,Caston, J.R.,Blaas, D.,Verdaguer, N. (deposition date: 2011-09-01, release date: 2012-03-28, Last modification date: 2024-11-20)

Primary citation

Garriga, D.,Pickl-Herk, A.,Luque, D.,Wruss, J.,Caston, J.R.,Blaas, D.,Verdaguer, N.
Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid.
Plos Pathog., 8:e1002473-e1002473, 2012

PubMed Abstract: Upon attachment to their respective receptor, human rhinoviruses (HRVs) are internalized into the host cell via different pathways but undergo similar structural changes. This ultimately results in the delivery of the viral RNA into the cytoplasm for replication. To improve our understanding of the conformational modifications associated with the release of the viral genome, we have determined the X-ray structure at 3.0 Å resolution of the end-stage of HRV2 uncoating, the empty capsid. The structure shows important conformational changes in the capsid protomer. In particular, a hinge movement around the hydrophobic pocket of VP1 allows a coordinated shift of VP2 and VP3. This overall displacement forces a reorganization of the inter-protomer interfaces, resulting in a particle expansion and in the opening of new channels in the capsid core. These new breaches in the capsid, opening one at the base of the canyon and the second at the particle two-fold axes, might act as gates for the externalization of the VP1 N-terminus and the extrusion of the viral RNA, respectively. The structural comparison between native and empty HRV2 particles unveils a number of pH-sensitive amino acid residues, conserved in rhinoviruses, which participate in the structural rearrangements involved in the uncoating process.

PubMed: 22241997
DOI: 10.1371/journal.ppat.1002473

Experimental method

X-RAY DIFFRACTION (3 Å)