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| | <SX load='5zz8' size='340' side='right' viewer='molstar' caption='[[5zz8]], [[Resolution|resolution]] 3.75Å' scene=''> | | <SX load='5zz8' size='340' side='right' viewer='molstar' caption='[[5zz8]], [[Resolution|resolution]] 3.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zz8]] is a 51 chain structure with sequence from [http://en.wikipedia.org/wiki/Hhv-2 Hhv-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZZ8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zz8]] is a 51 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_2 Human alphaherpesvirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZZ8 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UL38, TRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2]), TRX2, UL18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2]), UL19, MCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2]), SCP, UL35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2]), UL17, CVC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2]), UL25, CVC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2]), UL36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10310 HHV-2])</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]] 3.75Å</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=5zz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz8 OCA], [http://pdbe.org/5zz8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zz8 RCSB], [http://www.ebi.ac.uk/pdbsum/5zz8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz8 ProSAT]</span></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=5zz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz8 OCA], [https://pdbe.org/5zz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zz8 RCSB], [https://www.ebi.ac.uk/pdbsum/5zz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D6PUY5_HHV2 D6PUY5_HHV2]] 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/SCP_HHV2H SCP_HHV2H]] 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. [[http://www.uniprot.org/uniprot/G9I260_HHV2 G9I260_HHV2]] 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/A0A0E3U2U0_HHV2 A0A0E3U2U0_HHV2]] 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/A0A1U9ZLV0_HHV2 A0A1U9ZLV0_HHV2]] 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/TRX2_HHV2H TRX2_HHV2H]] 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. [[http://www.uniprot.org/uniprot/G9I238_HHV2 G9I238_HHV2]] 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/G9I260_HHV2 G9I260_HHV2] 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] |
| | <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: Hhv-2]] | + | [[Category: Human alphaherpesvirus 2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, W Y]] | + | [[Category: Chen WY]] |
| - | [[Category: Gao, Q]] | + | [[Category: Gao Q]] |
| - | [[Category: Li, Y H]] | + | [[Category: Li YH]] |
| - | [[Category: Liu, H R]] | + | [[Category: Liu HR]] |
| - | [[Category: Rao, Z H]] | + | [[Category: Rao ZH]] |
| - | [[Category: Tang, H]] | + | [[Category: Tang H]] |
| - | [[Category: Wang, J L]] | + | [[Category: Wang JL]] |
| - | [[Category: Wang, J Z]] | + | [[Category: Wang JZ]] |
| - | [[Category: Wang, N]] | + | [[Category: Wang N]] |
| - | [[Category: Wang, X X]] | + | [[Category: Wang XX]] |
| - | [[Category: Yuan, S]] | + | [[Category: Yuan S]] |
| - | [[Category: Zhang, X Z]] | + | [[Category: Zhang XZ]] |
| - | [[Category: Zhu, D J]] | + | [[Category: Zhu DJ]] |
| - | [[Category: Capsid]]
| + | |
| - | [[Category: Capsid-vertex-specific component]]
| + | |
| - | [[Category: Herpes simplex virus 2]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
G9I260_HHV2 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]
Publication Abstract from PubMed
Herpes simplex viruses (HSVs) cause human oral and genital ulcer diseases. Patients with HSV-2 have a higher risk of acquiring a human immunodeficiency virus infection. HSV-2 is a member of the alpha-herpesvirinae subfamily that together with the beta- and gamma-herpesvirinae subfamilies forms the Herpesviridae family. Here, we report the cryo-electron microscopy structure of the HSV-2 C-capsid with capsid-vertex-specific component (CVSC) that was determined at 3.75 A using a block-based reconstruction strategy. We present atomic models of multiple conformers for the capsid proteins (VP5, VP23, VP19C, and VP26) and CVSC. Comparison of the HSV-2 homologs yields information about structural similarities and differences between the three herpesviruses sub-families and we identify alpha-herpesvirus-specific structural features. The hetero-pentameric CVSC, consisting of a UL17 monomer, a UL25 dimer and a UL36 dimer, is bound tightly by a five-helix bundle that forms extensive networks of subunit contacts with surrounding capsid proteins, which reinforce capsid stability.
Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component.,Wang J, Yuan S, Zhu D, Tang H, Wang N, Chen W, Gao Q, Li Y, Wang J, Liu H, Zhang X, Rao Z, Wang X Nat Commun. 2018 Sep 10;9(1):3668. doi: 10.1038/s41467-018-06078-4. PMID:30201968[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang J, Yuan S, Zhu D, Tang H, Wang N, Chen W, Gao Q, Li Y, Wang J, Liu H, Zhang X, Rao Z, Wang X. Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component. Nat Commun. 2018 Sep 10;9(1):3668. doi: 10.1038/s41467-018-06078-4. PMID:30201968 doi:http://dx.doi.org/10.1038/s41467-018-06078-4
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