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==Crystal structure and proteomics analysis of empty virus like particles of Cowpea mosaic virus==
<StructureSection load='5fmo' size='340' side='right'caption='[[5fmo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fmo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cowpea_mosaic_virus Cowpea mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FMO 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]] 2.3&#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=5fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fmo OCA], [https://pdbe.org/5fmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fmo RCSB], [https://www.ebi.ac.uk/pdbsum/5fmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fmo ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/POL2_CPMVS POL2_CPMVS] Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. Binds to GTP and to single-stranded RNA and single-stranded DNA in a non-sequence-specific manner.<ref>PMID:10049828</ref> <ref>PMID:15483261</ref> <ref>PMID:15165817</ref> <ref>PMID:14722313</ref>   The cleavable C-terminus of small coat protein seems to be involved in the packaging of the virion RNAs. Also seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.<ref>PMID:10049828</ref> <ref>PMID:15483261</ref> <ref>PMID:15165817</ref> <ref>PMID:14722313</ref> 
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== Publication Abstract from PubMed ==
Empty virus-like particles (eVLPs) of Cowpea mosaic virus (CPMV) are currently being utilized as reagents in various biomedical and nanotechnology applications. Here, we report the crystal structure of CPMV eVLPs determined using X-ray crystallography at 2.3 A resolution and compare it with previously reported cryo-electron microscopy (cryo-EM) of eVLPs and virion crystal structures. Although the X-ray and cryo-EM structures of eVLPs are mostly similar, there exist significant differences at the C terminus of the small (S) subunit. The intact C terminus of the S subunit plays a critical role in enabling the efficient assembly of CPMV virions and eVLPs, but undergoes proteolysis after particle formation. In addition, we report the results of mass spectrometry-based proteomics analysis of coat protein subunits from CPMV eVLPs and virions that identify the C termini of S subunits undergo proteolytic cleavages at multiple sites instead of a single cleavage site as previously observed.

Crystal Structure and Proteomics Analysis of Empty Virus-like Particles of Cowpea Mosaic Virus.,Huynh NT, Hesketh EL, Saxena P, Meshcheriakova Y, Ku YC, Hoang LT, Johnson JE, Ranson NA, Lomonossoff GP, Reddy VS Structure. 2016 Apr 5;24(4):567-75. doi: 10.1016/j.str.2016.02.011. Epub 2016 Mar, 24. PMID:27021160<ref>PMID:27021160</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cowpea mosaic virus]]
[[Category: Large Structures]]
[[Category: Hesketh EL]]
[[Category: Hoang L]]
[[Category: Huynh N]]
[[Category: Johnson JE]]
[[Category: Ku YC]]
[[Category: Lomonossoff GP]]
[[Category: Meshcheriakova Y]]
[[Category: Ranson NA]]
[[Category: Reddy VS]]
[[Category: Saxena P]]