6f2s: Difference between revisions
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<StructureSection load='6f2s' size='340' side='right' caption='[[6f2s]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6f2s' size='340' side='right' caption='[[6f2s]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6f2s]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2S FirstGlance]. <br> | <table><tr><td colspan='2'>[[6f2s]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Ayvv Ayvv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2S FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2s OCA], [http://pdbe.org/6f2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2s RCSB], [http://www.ebi.ac.uk/pdbsum/6f2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2s ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44560 AYVV])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2s OCA], [http://pdbe.org/6f2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2s RCSB], [http://www.ebi.ac.uk/pdbsum/6f2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2s ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/W5RUR4_9GEMI W5RUR4_9GEMI]] Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus.[RuleBase:RU363025] | [[http://www.uniprot.org/uniprot/W5RUR4_9GEMI W5RUR4_9GEMI]] Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus.[RuleBase:RU363025] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Geminiviruses are major plant pathogens that threaten food security globally. They have a unique architecture built from two incomplete icosahedral particles, fused to form a geminate capsid. However, despite their importance to agricultural economies and fundamental biological interest, the details of how this is realized in 3D remain unknown. Here we report the structure of Ageratum yellow vein virus at 3.3 A resolution, using single-particle cryo-electron microscopy, together with an atomic model that shows that the N-terminus of the single capsid protein (CP) adopts three different conformations essential for building the interface between geminate halves. Our map also contains density for ~7 bases of single-stranded DNA bound to each CP, and we show that the interactions between the genome and CPs are different at the interface than in the rest of the capsid. With additional mutagenesis data, this suggests a central role for DNA binding-induced conformational change in directing the assembly of geminate capsids. | |||
The 3.3 A structure of a plant geminivirus using cryo-EM.,Hesketh EL, Saunders K, Fisher C, Potze J, Stanley J, Lomonossoff GP, Ranson NA Nat Commun. 2018 Jun 18;9(1):2369. doi: 10.1038/s41467-018-04793-6. PMID:29915210<ref>PMID:29915210</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6f2s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ayvv]] | |||
[[Category: Fisher, C]] | [[Category: Fisher, C]] | ||
[[Category: Hesketh, E L]] | [[Category: Hesketh, E L]] | ||
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[[Category: Saunders, K]] | [[Category: Saunders, K]] | ||
[[Category: Stanley, J]] | [[Category: Stanley, J]] | ||
[[Category: Gemini]] | [[Category: Gemini]] | ||
[[Category: Geminivirus]] | [[Category: Geminivirus]] | ||
[[Category: Ssdna]] | [[Category: Ssdna]] | ||
[[Category: Virus]] | [[Category: Virus]] | ||
Revision as of 10:43, 4 July 2018
CryoEM structure of Ageratum Yellow Vein virus (AYVV)CryoEM structure of Ageratum Yellow Vein virus (AYVV)
Structural highlights
Function[W5RUR4_9GEMI] Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus.[RuleBase:RU363025] Publication Abstract from PubMedGeminiviruses are major plant pathogens that threaten food security globally. They have a unique architecture built from two incomplete icosahedral particles, fused to form a geminate capsid. However, despite their importance to agricultural economies and fundamental biological interest, the details of how this is realized in 3D remain unknown. Here we report the structure of Ageratum yellow vein virus at 3.3 A resolution, using single-particle cryo-electron microscopy, together with an atomic model that shows that the N-terminus of the single capsid protein (CP) adopts three different conformations essential for building the interface between geminate halves. Our map also contains density for ~7 bases of single-stranded DNA bound to each CP, and we show that the interactions between the genome and CPs are different at the interface than in the rest of the capsid. With additional mutagenesis data, this suggests a central role for DNA binding-induced conformational change in directing the assembly of geminate capsids. The 3.3 A structure of a plant geminivirus using cryo-EM.,Hesketh EL, Saunders K, Fisher C, Potze J, Stanley J, Lomonossoff GP, Ranson NA Nat Commun. 2018 Jun 18;9(1):2369. doi: 10.1038/s41467-018-04793-6. PMID:29915210[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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