5a8t: Difference between revisions
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==Crystal structure of Antheraea mylitta CPV4 polyhedra type 2== | ==Crystal structure of Antheraea mylitta CPV4 polyhedra type 2== | ||
<StructureSection load='5a8t' size='340' side='right' caption='[[5a8t]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5a8t' size='340' side='right'caption='[[5a8t]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a8t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8T OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5a8t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Antheraea_mylitta_cypovirus_4 Antheraea mylitta cypovirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A8T FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.003Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8t OCA], [https://pdbe.org/5a8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a8t RCSB], [https://www.ebi.ac.uk/pdbsum/5a8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q67G25_9VIRU Q67G25_9VIRU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 5a8t" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Polyhedrin|Polyhedrin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Antheraea mylitta cypovirus 4]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Axford D]] | ||
[[Category: | [[Category: Evans G]] | ||
[[Category: | [[Category: Ginn HM]] | ||
[[Category: | [[Category: Ji X]] | ||
[[Category: | [[Category: Owen R]] | ||
[[Category: | [[Category: Stuart DI]] | ||
[[Category: | [[Category: Sutton G]] | ||
Latest revision as of 14:05, 10 January 2024
Crystal structure of Antheraea mylitta CPV4 polyhedra type 2Crystal structure of Antheraea mylitta CPV4 polyhedra type 2
Structural highlights
FunctionPublication Abstract from PubMedPolyhedra 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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