5a8u

Crystal structure of Orgyia pseudotsugata CPV5 polyhedra

spinqualitylabelsall models 5a8u, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a8u is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ACE Related: 5a8s, 5a8t, 5a8v, 5a96, 5a98, 5a99, 5a9a, 5a9b, 5a9c Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PYHD_CPVOP] Major component of the virus occlusion bodies, which are large proteinaceous structures (polyhedra), that protect the virus from the outside environment for extended periods until they are ingested by insect larvae. Publication Abstract from PubMed Polyhedra represent an ancient system used by a number of insect viruses to protect virions during long periods of environmental exposure. We present high resolution crystal structures of polyhedra for seven previously uncharacterised types of cypoviruses, four using ab initio selenomethionine phasing (two of these required over 100 selenomethionine crystals each). Approximately 80% of residues are structurally equivalent between all polyhedrins (pairwise rmsd 1.5A), whilst pairwise sequence identities, based on structural alignment, are as little as 12%. These structures illustrate the effect of 400million years of evolution on a system where the crystal lattice is the functionally conserved feature in the face of massive sequence variability. The conservation of crystal contacts is maintained across most of the molecular surface, except for a dispensable virus recognition domain. By spreading the contacts over so much of the protein surface the lattice remains robust in the face of many individual changes. Overall these unusual structural constraints seem to have skewed the molecule's evolution so that surface residues are almost as conserved as the internal residues. Polyhedra structures and the evolution of the insect viruses.,Ji X, Axford D, Owen R, Evans G, Ginn HM, Sutton G, Stuart DI J Struct Biol. 2015 Aug 18. pii: S1047-8477(15)30047-2. doi:, 10.1016/j.jsb.2015.08.009. PMID:26291392 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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