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| | <StructureSection load='5j36' size='340' side='right'caption='[[5j36]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='5j36' size='340' side='right'caption='[[5j36]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j36]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bfdv Bfdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J36 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5J36 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j36]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Beak_and_feather_disease_virus Beak and feather disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J36 FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j37|5j37]], [[5j09|5j09]]</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=5j36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j36 OCA], [https://pdbe.org/5j36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j36 RCSB], [https://www.ebi.ac.uk/pdbsum/5j36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j36 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77856 BFDV])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5j36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j36 OCA], [http://pdbe.org/5j36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j36 RCSB], [http://www.ebi.ac.uk/pdbsum/5j36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j36 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A023R6W2_BFDV A0A023R6W2_BFDV] |
| | <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: Bfdv]] | + | [[Category: Beak and feather disease virus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aragao, D]] | + | [[Category: Aragao D]] |
| - | [[Category: Forwood, J K]] | + | [[Category: Forwood JK]] |
| - | [[Category: Raidal, S]] | + | [[Category: Raidal S]] |
| - | [[Category: Sarker, S]] | + | [[Category: Sarker S]] |
| - | [[Category: Bfdv virus capsid jelly roll]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
A0A023R6W2_BFDV
Publication Abstract from PubMed
The assembly and regulation of viral capsid proteins into highly ordered macromolecular complexes is essential for viral replication. Here, we utilize crystal structures of the capsid protein from the smallest and simplest known viruses capable of autonomously replicating in animal cells, circoviruses, to establish structural and mechanistic insights into capsid morphogenesis and regulation. The beak and feather disease virus, like many circoviruses, encode only two genes: a capsid protein and a replication initiation protein. The capsid protein forms distinct macromolecular assemblies during replication and here we elucidate these structures at high resolution, showing that these complexes reverse the exposure of the N-terminal arginine rich domain responsible for DNA binding and nuclear localization. We show that assembly of these complexes is regulated by single-stranded DNA (ssDNA), and provide a structural basis of capsid assembly around single-stranded DNA, highlighting novel binding interfaces distinct from the highly positively charged N-terminal ARM domain.
Structural insights into the assembly and regulation of distinct viral capsid complexes.,Sarker S, Terron MC, Khandokar Y, Aragao D, Hardy JM, Radjainia M, Jimenez-Zaragoza M, de Pablo PJ, Coulibaly F, Luque D, Raidal SR, Forwood JK Nat Commun. 2016 Oct 4;7:13014. doi: 10.1038/ncomms13014. PMID:27698405[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sarker S, Terron MC, Khandokar Y, Aragao D, Hardy JM, Radjainia M, Jimenez-Zaragoza M, de Pablo PJ, Coulibaly F, Luque D, Raidal SR, Forwood JK. Structural insights into the assembly and regulation of distinct viral capsid complexes. Nat Commun. 2016 Oct 4;7:13014. doi: 10.1038/ncomms13014. PMID:27698405 doi:http://dx.doi.org/10.1038/ncomms13014
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