4llf: Difference between revisions
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==Crystal structure of Cucumber Necrosis Virus== | ==Crystal structure of Cucumber Necrosis Virus== | ||
<StructureSection load='4llf' size='340' side='right' caption='[[4llf]], [[Resolution|resolution]] 2.89Å' scene=''> | <StructureSection load='4llf' size='340' side='right'caption='[[4llf]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4llf]] is a 15 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4llf]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucumber_necrosis_virus Cucumber necrosis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LLF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8891Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4llf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llf OCA], [https://pdbe.org/4llf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4llf RCSB], [https://www.ebi.ac.uk/pdbsum/4llf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4llf ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CAPSD_CNV CAPSD_CNV] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cucumber necrosis virus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Smith T]] | ||
Latest revision as of 19:20, 20 September 2023
Crystal structure of Cucumber Necrosis VirusCrystal structure of Cucumber Necrosis Virus
Structural highlights
FunctionCAPSD_CNV Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. Publication Abstract from PubMedCucumber Necrosis Virus (CNV) is a member of the genus Tombusvirus and has a monopartite positive-sense RNA genome packaged in a T=3 icosahedral particle. CNV is transmitted in nature via zoospores of the fungus Olpidium bornovanus. CNV undergoes a conformational change upon binding to the zoospore that is required for transmission, and specific polysaccharides on the zoospore surface have been implicated in binding. To better understand this transmission process, we have determined the atomic structure of CNV. As expected, being a member of the Tombusvirus genus, the core structure of CNV is highly similar to that of Tomato bushy stunt virus (TBSV), with major differences lying on the exposed loops. Also, as was seen with TBSV, CNV appears to have a calcium binding site between the subunits around the quasi-3-fold axes. However, unlike TBSV, there appears to be a novel zinc binding site within the beta annulus formed by the N termini of the three C subunits at the icosahedral 3-fold axes. Two of the mutations causing defective transmission map immediately around this zinc binding site. The other mutations causing defective transmission and particle formation are mapped onto the CNV structure, and it is likely that a number of the mutations affect zoospore transmission by affecting conformational transitions rather than directly affecting receptor binding. Atomic structure of cucumber necrosis virus and the role of the capsid in vector transmission.,Li M, Kakani K, Katpally U, Johnson S, Rochon D, Smith TJ J Virol. 2013 Nov;87(22):12166-75. doi: 10.1128/JVI.01965-13. Epub 2013 Sep 4. PMID:24006433[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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