3LOB

Crystal Structure of Flock House Virus calcium mutant

Summary for 3LOB

• Entry DOI: 10.2210/pdb3lob/pdb
• Related: 1F8V 1NOV 2Q23 2Q25 2Q26 2Z2Q
• Descriptor: Coat protein beta, Coat protein gamma, RNA (5'-R(*UP*UP*U*AP*UP*CP*UP*(P))-3'), ... (4 entities in total)
• Functional Keywords: virus, flock house virus, rna, beta-barrel, jellyroll, aspartyl protease, capsid protein, hydrolase, protease, virion, icosahedral virus
• Biological source: Flock house virus (FHV); More
• Cellular location: Capsid protein beta: Virion (Potential). Peptide gamma: Virion (Potential): P12870 P12870
• Total number of polymer chains: 7
• Total formula weight: 134254.29

Authors

Johnson, J.E.,Banerjee, M.,Speir, J.A.,Huang, R. (deposition date: 2010-02-03, release date: 2010-04-21, Last modification date: 2024-11-20)

Primary citation

Banerjee, M.,Speir, J.A.,Kwan, M.H.,Huang, R.,Aryanpur, P.P.,Bothner, B.,Johnson, J.E.
Structure and function of a genetically engineered mimic of a nonenveloped virus entry intermediate.
J.Virol., 84:4737-4746, 2010

PubMed Abstract: Divalent metal ions are components of numerous icosahedral virus capsids. Flock House virus (FHV), a small RNA virus of the family Nodaviridae, was utilized as an accessible model system with which to address the effects of metal ions on capsid structure and on the biology of virus-host interactions. Mutations at the calcium-binding sites affected FHV capsid stability and drastically reduced virus infectivity, without altering the overall architecture of the capsid. The mutations also altered the conformation of gamma, a membrane-disrupting, virus-encoded peptide usually sequestered inside the capsid, by increasing its exposure under neutral pH conditions. Our data demonstrate that calcium binding is essential for maintaining a pH-based control on gamma exposure and host membrane disruption, and they reveal a novel rationale for the metal ion requirement during virus entry and infectivity. In the light of the phenotypes displayed by a calcium site mutant of FHV, we suggest that this mutant corresponds to an early entry intermediate formed in the endosomal pathway.

PubMed: 20164221
DOI: 10.1128/JVI.02670-09

Experimental method

X-RAY DIFFRACTION (3.6 Å)