6od7: Difference between revisions

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'''Unreleased structure'''


The entry 6od7 is ON HOLD
==Herpes simplex virus type 1 (HSV-1) pUL6 portal protein, dodecameric complex==
<StructureSection load='6od7' size='340' side='right'caption='[[6od7]], [[Resolution|resolution]] 5.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6od7]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1_strain_kos Human herpesvirus 1  strain kos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OD7 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=6od7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6od7 OCA], [http://pdbe.org/6od7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6od7 RCSB], [http://www.ebi.ac.uk/pdbsum/6od7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6od7 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/H9E912_HHV1 H9E912_HHV1]] Forms a portal in the viral capsid through which viral DNA is translocated during DNA packaging. Assembles as a dodecamer at a single fivefold axe of the T=16 icosahedric capsid. Binds to the molecular motor that translocates the viral DNA, termed terminase.[HAMAP-Rule:MF_04012]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Herpesviruses are enveloped viruses that are prevalent in the human population and are responsible for diverse pathologies, including cold sores, birth defects and cancers. They are characterized by a highly pressurized pseudo-icosahedral capsid-with triangulation number (T) equal to 16-encapsidating a tightly packed double-stranded DNA (dsDNA) genome(1-3). A key process in the herpesvirus life cycle involves the recruitment of an ATP-driven terminase to a unique portal vertex to recognize, package and cleave concatemeric dsDNA, ultimately giving rise to a pressurized, genome-containing virion(4,5). Although this process has been studied in dsDNA phages(6-9)-with which herpesviruses bear some similarities-a lack of high-resolution in situ structures of genome-packaging machinery has prevented the elucidation of how these multi-step reactions, which require close coordination among multiple actors, occur in an integrated environment. To better define the structural basis of genome packaging and organization in herpes simplex virus type 1 (HSV-1), we developed sequential localized classification and symmetry relaxation methods to process cryo-electron microscopy (cryo-EM) images of HSV-1 virions, which enabled us to decouple and reconstruct hetero-symmetric and asymmetric elements within the pseudo-icosahedral capsid. Here we present in situ structures of the unique portal vertex, genomic termini and ordered dsDNA coils in the capsid spooled around a disordered dsDNA core. We identify tentacle-like helices and a globular complex capping the portal vertex that is not observed in phages, indicative of herpesvirus-specific adaptations in the DNA-packaging process. Finally, our atomic models of portal vertex elements reveal how the fivefold-related capsid accommodates symmetry mismatch imparted by the dodecameric portal-a longstanding mystery in icosahedral viruses-and inform possible DNA-sequence recognition and headful-sensing pathways involved in genome packaging. This work showcases how to resolve symmetry-mismatched elements in a large eukaryotic virus and provides insights into the mechanisms of herpesvirus genome packaging.


Authors:  
Cryo-EM structures of herpes simplex virus type 1 portal vertex and packaged genome.,Liu YT, Jih J, Dai X, Bi GQ, Zhou ZH Nature. 2019 Jun;570(7760):257-261. doi: 10.1038/s41586-019-1248-6. Epub 2019 May, 29. PMID:31142842<ref>PMID:31142842</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6od7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human herpesvirus 1 strain kos]]
[[Category: Large Structures]]
[[Category: Bi, G Q]]
[[Category: Dai, X H]]
[[Category: Jih, J]]
[[Category: Liu, Y T]]
[[Category: Zhou, Z H]]
[[Category: Dna-packaging]]
[[Category: Dna-translocation]]
[[Category: Dodecamer]]
[[Category: Portal]]
[[Category: Viral protein]]