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| | <SX load='6cgr' size='340' side='right' viewer='molstar' caption='[[6cgr]], [[Resolution|resolution]] 4.20Å' scene=''> | | <SX load='6cgr' size='340' side='right' viewer='molstar' caption='[[6cgr]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cgr]] is a 51 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CGR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cgr]] is a 51 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGR 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=6cgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgr OCA], [http://pdbe.org/6cgr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgr RCSB], [http://www.ebi.ac.uk/pdbsum/6cgr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgr 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]] 4.2Å</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=6cgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgr OCA], [https://pdbe.org/6cgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgr RCSB], [https://www.ebi.ac.uk/pdbsum/6cgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G8HBD8_HHV1 G8HBD8_HHV1]] Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP.[HAMAP-Rule:MF_04025] [[http://www.uniprot.org/uniprot/G8H8D9_HHV1 G8H8D9_HHV1]] 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/G8HBD2_HHV1 G8HBD2_HHV1]] 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] [[http://www.uniprot.org/uniprot/F8REX2_HHV1 F8REX2_HHV1]] 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/G8HBF0_HHV1 G8HBF0_HHV1]] Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein.[HAMAP-Rule:MF_04044] [[http://www.uniprot.org/uniprot/Q25BW6_HHV1 Q25BW6_HHV1]] 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_04020] [[http://www.uniprot.org/uniprot/F8RFA1_HHV1 F8RFA1_HHV1]] Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes.[HAMAP-Rule:MF_04017] | + | [https://www.uniprot.org/uniprot/G8HBD2_HHV11 G8HBD2_HHV11] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Human herpesvirus 1]] | + | [[Category: Human alphaherpesvirus 1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dai, X H]] | + | [[Category: Dai XH]] |
| - | [[Category: Zhou, Z H]] | + | [[Category: Zhou ZH]] |
| - | [[Category: Capsid-associated tegument complex]]
| + | |
| - | [[Category: Herpes simplex virus type 1]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
G8HBD2_HHV11
Publication Abstract from PubMed
Herpes simplex viruses (HSVs) rely on capsid-associated tegument complex (CATC) for long-range axonal transport of their genome-containing capsids between sites of infection and neuronal cell bodies. Here we report cryo-electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers of capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. Crowning every capsid vertex are five copies of heteropentameric CATC, each containing a pUL17 monomer supporting the coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear capsid egress and axonal capsid transport. Notwithstanding newly discovered fold conservation between triplex proteins and bacteriophage lambda protein gpD and the previously recognized bacteriophage HK97 gp5-like fold in VP5, HSV-1 capsid proteins exhibit extraordinary diversity in forms of domain insertion and conformational polymorphism, not only for interactions with tegument proteins but also for encapsulation of large genomes.
Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.,Dai X, Zhou ZH Science. 2018 Apr 6;360(6384). pii: 360/6384/eaao7298. doi:, 10.1126/science.aao7298. Epub 2018 Apr 5. PMID:29622628[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dai X, Zhou ZH. Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes. Science. 2018 Apr 6;360(6384). pii: 360/6384/eaao7298. doi:, 10.1126/science.aao7298. Epub 2018 Apr 5. PMID:29622628 doi:http://dx.doi.org/10.1126/science.aao7298
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