1SLQ

Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT

Summary for 1SLQ

• Entry DOI: 10.2210/pdb1slq/pdb
• Related: 1KQR 1KRI
• Descriptor: VP4 (1 entity in total)
• Functional Keywords: beta sandwich, greek key, alpha helical triple coiled-coil, membrane penetration protein, non-enveloped virus, spike protein, viral protein
• Biological source: Rhesus rotavirus
• Total number of polymer chains: 6
• Total formula weight: 187847.67

Authors

Dormitzer, P.R.,Nason, E.B.,Prasad, B.V.V.,Harrison, S.C. (deposition date: 2004-03-06, release date: 2004-08-31, Last modification date: 2024-02-14)

Primary citation

Dormitzer, P.R.,Nason, E.B.,Prasad, B.V.,Harrison, S.C.
Structural rearrangements in the membrane penetration protein of a non-enveloped virus.
Nature, 430:1053-1058, 2004

PubMed Abstract: Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes. We have determined the crystal structure, at 3.2 A resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a approximately 12 A resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses.

PubMed: 15329727
DOI: 10.1038/nature02836

Experimental method

X-RAY DIFFRACTION (3.2 Å)