X-ray crystallographic structure of the Norwalk virus capsid.

Academic Article

Abstract

  • Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded beta-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor-Tu. This subdomain, located at the exterior of the capsid, has the largest sequence variation among Norwalk-like human caliciviruses and is likely to contain the determinants of strain specificity and cell binding.
  • Authors

    Published In

  • Science  Journal
  • Keywords

  • Amino Acid Sequence, Capsid, Capsid Proteins, Cryoelectron Microscopy, Crystallography, X-Ray, Dimerization, Genome, Viral, Humans, Hydrogen Bonding, Image Processing, Computer-Assisted, Models, Molecular, Molecular Sequence Data, Norwalk virus, Protein Conformation, Protein Folding, Protein Structure, Secondary, Recombinant Proteins, Virus Assembly
  • Author List

  • Prasad BV; Hardy ME; Dokland T; Bella J; Rossmann MG; Estes MK
  • Start Page

  • 287
  • End Page

  • 290
  • Volume

  • 286
  • Issue

  • 5438