View source for 5a9a


==Crystal structure of Simulium ubiquitum CPV20 polyhedra==
<StructureSection load='5a9a' size='340' side='right'caption='[[5a9a]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a9a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simulium_ubiquitum_cypovirus Simulium ubiquitum cypovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9A 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]] 1.822&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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=5a9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9a OCA], [https://pdbe.org/5a9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9a RCSB], [https://www.ebi.ac.uk/pdbsum/5a9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0MX25_9REOV Q0MX25_9REOV] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5a9a" style="background-color:#fffaf0;"></div>

==See Also==
*[[Polyhedrin|Polyhedrin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Simulium ubiquitum cypovirus]]
[[Category: Axford D]]
[[Category: Evans G]]
[[Category: Ginn HM]]
[[Category: Ji X]]
[[Category: Owen R]]
[[Category: Stuart DI]]
[[Category: Sutton G]]