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.

6ppd

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Kaposi's sarcoma-associated herpesvirus (KSHV), C1 penton vertex register, CATC-absent structure

6ppd, resolution 3.70Å

Structural highlights

6ppd is a 16 chain structure with sequence from Human herpesvirus 8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	6ppb
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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] [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] [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] [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]

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gong D, Dai X, Jih J, Liu YT, Bi GQ, Sun R, Zhou ZH. DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV. Cell. 2019 Sep 5;178(6):1329-1343.e12. doi: 10.1016/j.cell.2019.07.035. Epub 2019, Aug 22. PMID:31447177 doi:http://dx.doi.org/10.1016/j.cell.2019.07.035

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ppd"

@@ Line 3: / Line 3: @@
 <SX load='6ppd' size='340' side='right' viewer='molstar' caption='[[6ppd]], [[Resolution|resolution]] 3.70&Aring;' 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>
+<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://proteopedia.org/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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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 ==

6ppd

From Proteopedia

Current revision

Kaposi's sarcoma-associated herpesvirus (KSHV), C1 penton vertex register, CATC-absent structure

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox