1IHM

CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID

Summary for 1IHM

• Entry DOI: 10.2210/pdb1ihm/pdb
• Descriptor: capsid protein (1 entity in total)
• Functional Keywords: beta-barrel, ef-tu-like domain caliciviridae, t=3 icosahedral capsid, icosahedral virus, virus
• Biological source: Norwalk virus
• Cellular location: Virion: Q83884
• Total number of polymer chains: 3
• Total formula weight: 169889.48

Authors

Prasad, B.V.,Hardy, M.E.,Dokland, T.,Bella, J.,Rossmann, M.G.,Estes, M.K. (deposition date: 2001-04-19, release date: 2001-05-16, Last modification date: 2024-04-03)

Primary citation

Prasad, B.V.,Hardy, M.E.,Dokland, T.,Bella, J.,Rossmann, M.G.,Estes, M.K.
X-ray crystallographic structure of the Norwalk virus capsid
Science, 286:287-290, 1999

PubMed 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.

PubMed: 10514371
DOI: 10.1126/science.286.5438.287

Experimental method

X-RAY DIFFRACTION (3.4 Å)