View source for 3izx


==3.1 Angstrom cryoEM structure of cytoplasmic polyhedrosis virus==
<SX load='3izx' size='340' side='right' viewer='molstar' caption='[[3izx]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3izx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori_cypovirus_1 Bombyx mori cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</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=3izx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izx OCA], [https://pdbe.org/3izx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3izx RCSB], [https://www.ebi.ac.uk/pdbsum/3izx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3izx ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/CAPSD_CPVBM CAPSD_CPVBM] Capsid protein self-assembles to form an icosahedral capsid with a pseudo T=2 symmetry, about 50 nm in diameter, and consisting of 120 capsid proteins. The capsid encapsulates the genomic RNA.
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== Publication Abstract from PubMed ==
Unlike the multishelled viruses in the Reoviridae, cytoplasmic polyhedrosis virus (CPV) is single shelled, yet stable and fully capable of carrying out functions conserved within Reoviridae. Here, we report a 3.1 A resolution cryo electron microscopy structure of CPV and derive its atomic model, consisting of 60 turret proteins (TPs), 120 each of capsid shell proteins (CSPs) and large protrusion proteins (LPPs). Two unique segments of CSP contribute to CPV's stability: an inserted protrusion domain interacting with neighboring proteins, and an N-anchor tying up CSPs together through strong interactions such as beta sheet augmentation. Without the need to interact with outer shell proteins, LPP retains only the N-terminal two-third region containing a conserved helix-barrel core and interacts exclusively with CSP. TP is also simplified, containing only domains involved in RNA capping. Our results illustrate how CPV proteins have evolved in a coordinative manner to economically carry out their conserved functions.

Atomic Model of CPV Reveals the Mechanism Used by This Single-Shelled Virus to Economically Carry Out Functions Conserved in Multishelled Reoviruses.,Yu X, Ge P, Jiang J, Atanasov I, Zhou ZH Structure. 2011 May 11;19(5):652-61. PMID:21565700<ref>PMID:21565700</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
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[[Category: Bombyx mori cypovirus 1]]
[[Category: Large Structures]]
[[Category: Atanasov I]]
[[Category: Ge P]]
[[Category: Jiang J]]
[[Category: Yu X]]
[[Category: Zhou ZH]]