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2WUX

the crystal structure of recombinant baculovirus polyhedra

Summary for 2WUX
Entry DOI10.2210/pdb2wux/pdb
Related2WUY
DescriptorPOLYHEDRIN (2 entities in total)
Functional Keywordsmicrocrystals, polyhedra, viral protein, viral occlusion body, viral capsid
Biological sourceAUTOGRAPHA CALIFORNICA NUCLEAR POLYHEDROSIS VIRUS
Total number of polymer chains1
Total formula weight28736.76
Authors
Ji, X.,Sutton, G.,Evans, G.,Axford, D.,Owen, R.,Stuart, D.I. (deposition date: 2009-10-10, release date: 2009-12-15, Last modification date: 2011-07-13)
Primary citationJi, X.,Sutton, G.,Evans, G.,Axford, D.,Owen, R.,Stuart, D.I.
How Baculovirus Polyhedra Fit Square Pegs Into Round Holes to Robustly Package Viruses.
Embo J., 29:505-, 2010
Cited by
PubMed Abstract: Natural protein crystals (polyhedra) armour certain viruses, allowing them to survive for years under hostile conditions. We have determined the structure of polyhedra of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), revealing a highly symmetrical covalently cross-braced robust lattice, the subunits of which possess a flexible adaptor enabling this supra-molecular assembly to specifically entrap massive baculoviruses. Inter-subunit chemical switches modulate the controlled release of virus particles in the unusual high pH environment of the target insect's gut. Surprisingly, the polyhedrin subunits are more similar to picornavirus coat proteins than to the polyhedrin of cytoplasmic polyhedrosis virus (CPV). It is, therefore, remarkable that both AcMNPV and CPV polyhedra possess identical crystal lattices and crystal symmetry. This crystalline arrangement must be particularly well suited to the functional requirements of the polyhedra and has been either preserved or re-selected during evolution. The use of flexible adaptors to generate a powerful system for packaging irregular particles is characteristic of the AcMNPV polyhedrin and may provide a vehicle to sequester a wide range of objects such as biological nano-particles.
PubMed: 19959989
DOI: 10.1038/EMBOJ.2009.352
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.838 Å)
Structure validation

226707

數據於2024-10-30公開中

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