3KXS

Crystal structure of HBV capsid mutant dimer (oxy form), strain adyw

Summary for 3KXS

• Entry DOI: 10.2210/pdb3kxs/pdb
• Related: 2G33 2G34
• Descriptor: Capsid protein (2 entities in total)
• Functional Keywords: core protein, capsid, hepadnavirus, four helix bundle, icosahedral, dimer, capsid protein, dna-binding, host cytoplasm, host-virus interaction, phosphoprotein, rna-binding, virion, viral protein
• Biological source: Hepatitis B virus subtype adyw (HBV-D)
• Cellular location: Capsid protein: Virion: P03147
• Total number of polymer chains: 6
• Total formula weight: 96392.18

Authors

Packianathan, C.,Katen, S.P.,Zlotnick, A. (deposition date: 2009-12-03, release date: 2010-02-02, Last modification date: 2024-11-06)

Primary citation

Packianathan, C.,Katen, S.P.,Dann, C.E.,Zlotnick, A.
Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly
J.Virol., 84:1607-1615, 2010

PubMed Abstract: In infected cells, virus components must be organized at the right place and time to ensure assembly of infectious virions. From a different perspective, assembly must be prevented until all components are available. Hypothetically, this can be achieved by allosterically controlling assembly. Consistent with this hypothesis, here we show that the structure of the hepatitis B virus (HBV) core protein dimer, which can spontaneously self-assemble, is incompatible with capsid assembly. Systematic differences between core protein dimer and capsid conformations demonstrate linkage between the intradimer interface and interdimer contact surface. These structures also provide explanations for the capsid-dimer selectivity of some antibodies and the activities of assembly effectors. Solution studies suggest that the assembly-inactive state is more accurately an ensemble of conformations. Simulations show that allostery supports controlled assembly and results in capsids that are resistant to dissociation. We propose that allostery, as demonstrated in HBV, is common to most self-assembling viruses.

PubMed: 19939922
DOI: 10.1128/JVI.02033-09

Experimental method

X-RAY DIFFRACTION (2.25 Å)