5a98: Difference between revisions
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==Crystal structure of Trichoplusia ni CPV15 polyhedra== | |||
<StructureSection load='5a98' size='340' side='right'caption='[[5a98]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a98]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoplusia_ni_cypovirus_15 Trichoplusia ni cypovirus 15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A98 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.816Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a98 OCA], [https://pdbe.org/5a98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a98 RCSB], [https://www.ebi.ac.uk/pdbsum/5a98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a98 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9ELS6_9VIRU Q9ELS6_9VIRU] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:26291392</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[ | </div> | ||
[[Category: | <div class="pdbe-citations 5a98" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Axford | ==See Also== | ||
[[Category: | *[[Polyhedrin|Polyhedrin]] | ||
[[Category: Ginn | == References == | ||
[[Category: | <references/> | ||
[[Category: Owen | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Trichoplusia ni cypovirus 15]] | |||
[[Category: Axford D]] | |||
[[Category: Evans G]] | |||
[[Category: Ginn HM]] | |||
[[Category: Ji X]] | |||
[[Category: Owen R]] | |||
[[Category: Stuart DI]] | |||
[[Category: Sutton G]] | |||