This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


7bqt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:49, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='7bqt' size='340' side='right'caption='[[7bqt]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
<StructureSection load='7bqt' size='340' side='right'caption='[[7bqt]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7bqt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Epstein-barr_virus_(strain_b95-8) Epstein-barr virus (strain b95-8)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BQT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BQT FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7bqt]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BQT FirstGlance]. <br>
-
</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=7bqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqt OCA], [http://pdbe.org/7bqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bqt RCSB], [http://www.ebi.ac.uk/pdbsum/7bqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqt ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.8&#8491;</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=7bqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqt OCA], [https://pdbe.org/7bqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bqt RCSB], [https://www.ebi.ac.uk/pdbsum/7bqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PORTL_EBVB9 PORTL_EBVB9]] 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]
+
[https://www.uniprot.org/uniprot/PORTL_EBVB9 PORTL_EBVB9] 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 ==
+
-
Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection.
+
-
 
+
-
CryoEM structure of the tegumented capsid of Epstein-Barr virus.,Li Z, Zhang X, Dong L, Pang J, Xu M, Zhong Q, Zeng MS, Yu X Cell Res. 2020 Jul 3. pii: 10.1038/s41422-020-0363-0. doi:, 10.1038/s41422-020-0363-0. PMID:32620850<ref>PMID:32620850</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 7bqt" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Portal protein|Portal protein]]
+
*[[Portal protein 3D structures|Portal protein 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Human herpesvirus 4 strain B95-8]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Li, Z]]
+
[[Category: Li Z]]
-
[[Category: Yu, X]]
+
[[Category: Yu X]]
-
[[Category: Epstein-barr virus]]
+
-
[[Category: Portal dodecomer]]
+
-
[[Category: Tegumented capsid]]
+
-
[[Category: Viral protein]]
+

Current revision

Epstein-Barr virus, C12 portal dodecamer

PDB ID 7bqt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7bqt"
Personal tools