5j09
From Proteopedia
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<table><tr><td colspan='2'>[[5j09]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J09 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5j09]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J09 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j36|5j36]], [[5j37|5j37]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j36|5j36]], [[5j37|5j37]]</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=5j09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j09 OCA], [http://pdbe.org/5j09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j09 RCSB], [http://www.ebi.ac.uk/pdbsum/5j09 PDBsum]</span></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=5j09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j09 OCA], [http://pdbe.org/5j09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j09 RCSB], [http://www.ebi.ac.uk/pdbsum/5j09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j09 ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:27698405</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5j09" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:10, 19 October 2016
Crystal structure of decameric BFDV Capsid Protein
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