6ppd: Difference between revisions
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The | ==Kaposi's sarcoma-associated herpesvirus (KSHV), C1 penton vertex register, CATC-absent structure== | ||
<StructureSection load='6ppd' size='340' side='right'caption='[[6ppd]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ppd]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PPD FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ppb|6ppb]]</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=6ppd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ppd OCA], [http://pdbe.org/6ppd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ppd RCSB], [http://www.ebi.ac.uk/pdbsum/6ppd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ppd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/C7E5A9_HHV8 C7E5A9_HHV8]] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.[HAMAP-Rule:MF_04019] [[http://www.uniprot.org/uniprot/Q76RF4_HHV8 Q76RF4_HHV8]] Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly.[HAMAP-Rule:MF_04022] [[http://www.uniprot.org/uniprot/Q76RF6_HHV8 Q76RF6_HHV8]] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.[HAMAP-Rule:MF_04018] [[http://www.uniprot.org/uniprot/D0UZN7_HHV8 D0UZN7_HHV8]] Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.[HAMAP-Rule:MF_04016] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Assembly of Kaposi's sarcoma-associated herpesvirus (KSHV) begins at a bacteriophage-like portal complex that nucleates formation of an icosahedral capsid with capsid-associated tegument complexes (CATCs) and facilitates translocation of an approximately 150-kb dsDNA genome, followed by acquisition of a pleomorphic tegument and envelope. Because of deviation from icosahedral symmetry, KSHV portal and tegument structures have largely been obscured in previous studies. Using symmetry-relaxed cryo-EM, we determined the in situ structure of the KSHV portal and its interactions with surrounding capsid proteins, CATCs, and the terminal end of KSHV's dsDNA genome. Our atomic models of the portal and capsid/CATC, together with visualization of CATCs' variable occupancy and alternate orientation of CATC-interacting vertex triplexes, suggest a mechanism whereby the portal orchestrates procapsid formation and asymmetric long-range determination of CATC attachment during DNA packaging prior to pleomorphic tegumentation/envelopment. Structure-based mutageneses confirm that a triplex deep binding groove for CATCs is a hotspot that holds promise for antiviral development. | |||
DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV.,Gong D, Dai X, Jih J, Liu YT, Bi GQ, Sun R, Zhou ZH Cell. 2019 Sep 5;178(6):1329-1343.e12. doi: 10.1016/j.cell.2019.07.035. Epub 2019, Aug 22. PMID:31447177<ref>PMID:31447177</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ppd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human herpesvirus 8]] | |||
[[Category: Large Structures]] | |||
[[Category: Bi, G Q]] | |||
[[Category: Dai, X]] | |||
[[Category: Gong, D]] | |||
[[Category: Jih, J]] | |||
[[Category: Liu, Y T]] | |||
[[Category: Sun, R]] | |||
[[Category: Zhou, Z H]] | |||
[[Category: Capsid]] | |||
[[Category: Complex]] | |||
[[Category: Tegument]] | |||
[[Category: Vertex]] | |||
[[Category: Viral protein]] | |||
[[Category: Virus]] | |||