8g1r
From Proteopedia
(Difference between revisions)
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==A Vibrio cholerae viral satellite enables efficient horizontal transfer by using an external scaffold to assemble hijacked coat proteins into small capsids== | ==A Vibrio cholerae viral satellite enables efficient horizontal transfer by using an external scaffold to assemble hijacked coat proteins into small capsids== | ||
| - | < | + | <SX load='8g1r' size='340' side='right' viewer='molstar' caption='[[8g1r]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8g1r]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] and [https://en.wikipedia.org/wiki/Vibrio_phage_ICP1_2011_A Vibrio phage ICP1_2011_A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G1R FirstGlance]. <br> | <table><tr><td colspan='2'>[[8g1r]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] and [https://en.wikipedia.org/wiki/Vibrio_phage_ICP1_2011_A Vibrio phage ICP1_2011_A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G1R FirstGlance]. <br> | ||
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8g1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g1r OCA], [https://pdbe.org/8g1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g1r RCSB], [https://www.ebi.ac.uk/pdbsum/8g1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g1r ProSAT]</span></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=8g1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g1r OCA], [https://pdbe.org/8g1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g1r RCSB], [https://www.ebi.ac.uk/pdbsum/8g1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g1r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == | + | <div style="background-color:#fffaf0;"> |
| - | [ | + | == Publication Abstract from PubMed == |
| + | Phage satellites commonly remodel capsids they hijack from the phages they parasitize, but only a few mechanisms regulating the change in capsid size have been reported. Here, we investigated how a satellite from Vibrio cholerae, PLE, remodels the capsid it has been predicted to steal from the phage ICP1 (1). We identified that a PLE-encoded protein, TcaP, is both necessary and sufficient to form small capsids during ICP1 infection. Interestingly, we found that PLE is dependent on small capsids for efficient transduction of its genome, making it the first satellite to have this requirement. ICP1 isolates that escaped TcaP-mediated remodeling acquired substitutions in the coat protein, suggesting an interaction between these two proteins. With a procapsid-like-particle (PLP) assembly platform in Escherichia coli, we demonstrated that TcaP is a bona fide scaffold that regulates the assembly of small capsids. Further, we studied the structure of PLE PLPs using cryogenic electron microscopy and found that TcaP is an external scaffold, that is functionally and somewhat structurally similar to the external scaffold, Sid, encoded by the unrelated satellite P4 (2). Finally, we showed that TcaP is largely conserved across PLEs. Together, these data support a model in which TcaP directs the assembly of small capsids comprised of ICP1 coat proteins, which inhibits the complete packaging of the ICP1 genome and permits more efficient packaging of replicated PLE genomes. | ||
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| + | A Vibrio cholerae viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids.,Boyd CM, Subramanian S, Dunham DT, Parent KN, Seed KD bioRxiv [Preprint]. 2023 Sep 14:2023.03.01.530633. doi: , 10.1101/2023.03.01.530633. PMID:36909475<ref>PMID:36909475</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8g1r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
Current revision
A Vibrio cholerae viral satellite enables efficient horizontal transfer by using an external scaffold to assemble hijacked coat proteins into small capsids
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