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4WZN

CRYSTAL STRUCTURE OF THE 2B PROTEIN SOLUBLE DOMAIN FROM HEPATITIS A VIRUS

Summary for 4WZN
Entry DOI10.2210/pdb4wzn/pdb
DescriptorGenome polyprotein, GLYCEROL (3 entities in total)
Functional Keywordsfiber, viral recruitment machinery, viral protein, hepatitis a virus, non-structural protein
Biological sourceHuman hepatitis A virus genotype IB (isolate HM175) (HHAV)
Total number of polymer chains2
Total formula weight50475.87
Authors
Garriga, D.,Vives-Adrian, L.,Buxaderas, M.,Ferreira-da-Silva, F.,Almeida, B.,Macedo-Ribeiro, S.,Pereira, P.J.,Verdaguer, N. (deposition date: 2014-11-20, release date: 2015-01-28, Last modification date: 2024-05-08)
Primary citationVives-Adrian, L.,Garriga, D.,Buxaderas, M.,Fraga, J.,Pereira, P.J.,Macedo-Ribeiro, S.,Verdaguer, N.
Structural Basis for Host Membrane Remodeling Induced by Protein 2B of Hepatitis A Virus.
J.Virol., 89:3648-3658, 2015
Cited by
PubMed Abstract: The complexity of viral RNA synthesis and the numerous participating factors require a mechanism to topologically coordinate and concentrate these multiple viral and cellular components, ensuring a concerted function. Similarly to all other positive-strand RNA viruses, picornaviruses induce rearrangements of host intracellular membranes to create structures that act as functional scaffolds for genome replication. The membrane-targeting proteins 2B and 2C, their precursor 2BC, and protein 3A appear to be primarily involved in membrane remodeling. Little is known about the structure of these proteins and the mechanisms by which they induce massive membrane remodeling. Here we report the crystal structure of the soluble region of hepatitis A virus (HAV) protein 2B, consisting of two domains: a C-terminal helical bundle preceded by an N-terminally curved five-stranded antiparallel β-sheet that displays striking structural similarity to the β-barrel domain of enteroviral 2A proteins. Moreover, the helicoidal arrangement of the protein molecules in the crystal provides a model for 2B-induced host membrane remodeling during HAV infection.
PubMed: 25589659
DOI: 10.1128/JVI.02881-14
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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