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| | ==HSV-1 nuclear egress complex== | | ==HSV-1 nuclear egress complex== |
| - | <StructureSection load='4zxs' size='340' side='right' caption='[[4zxs]], [[Resolution|resolution]] 2.77Å' scene=''> | + | <StructureSection load='4zxs' size='340' side='right'caption='[[4zxs]], [[Resolution|resolution]] 2.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zxs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZXS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zxs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZXS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.772Å</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=4zxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxs OCA], [http://pdbe.org/4zxs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zxs RCSB], [http://www.ebi.ac.uk/pdbsum/4zxs PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4zxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxs OCA], [https://pdbe.org/4zxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zxs RCSB], [https://www.ebi.ac.uk/pdbsum/4zxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zxs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UL34_HHV11 UL34_HHV11]] Plays a major role in virion nuclear egress, the first step of virion release from infected cell. Viral capsids are initially assembled within the nucleus, UL31/UL34 complex induces capsids budding and envelopment into the perinuclear space. Then UL31/UL34 complex promotes fusion of perinuclear virion envelope with the outer nuclear membrane, releasing viral capsid into the cytoplasm where it will engages budding sites in the Golgi or trans-Golgi network.<ref>PMID:12805460</ref> <ref>PMID:15140953</ref> <ref>PMID:15140956</ref> [[http://www.uniprot.org/uniprot/UL31_HHV11 UL31_HHV11]] Plays a major role in virion nuclear egress, the first step of virion release from infected cell. Viral capsids are initially assembled within the nucleus, UL31/UL34 complex induces capsids budding and envelopment into the perinuclear space. Then UL31/UL34 complex promotes fusion of perinuclear virion envelope with the outer nuclear membrane, releasing viral capsid into the cytoplasm where it will engages budding sites in the Golgi or trans-Golgi network.<ref>PMID:15140953</ref> <ref>PMID:15140956</ref> | + | [https://www.uniprot.org/uniprot/NEC2_HHV11 NEC2_HHV11] Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.[HAMAP-Rule:MF_04024]<ref>PMID:12805460</ref> <ref>PMID:15140953</ref> <ref>PMID:15140956</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bigalke, J M]] | + | [[Category: Human alphaherpesvirus 1 strain 17]] |
| - | [[Category: Heldwein, E E]]
| + | [[Category: Large Structures]] |
| - | [[Category: Hsv-1]]
| + | [[Category: Bigalke JM]] |
| - | [[Category: Membrane deformation]] | + | [[Category: Heldwein EE]] |
| - | [[Category: Nuclear egress]] | + | |
| - | [[Category: Ul31]] | + | |
| - | [[Category: Ul34]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
NEC2_HHV11 Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.[HAMAP-Rule:MF_04024][1] [2] [3]
Publication Abstract from PubMed
During nuclear egress, herpesvirus capsids bud at the inner nuclear membrane forming perinuclear viral particles that subsequently fuse with the outer nuclear membrane, releasing capsids into the cytoplasm. This unusual budding process is mediated by the nuclear egress complex (NEC) composed of two conserved viral proteins, UL31 and UL34. Earlier, we discovered that the herpesvirus nuclear egress complex (NEC) could bud synthetic membranes in vitro without the help of other proteins by forming a coat-like hexagonal scaffold inside the budding membrane. To understand the structural basis of NEC-mediated membrane budding, we determined the crystal structures of the NEC from two herpesviruses. The hexagonal lattice observed in the NEC crystals recapitulates the honeycomb coats within the budded vesicles. Perturbation of the oligomeric interfaces through mutagenesis blocks budding in vitro confirming that NEC oligomerization into a honeycomb lattice drives budding. The structure represents the first atomic-level view of an oligomeric array formed by a membrane-deforming protein, making possible the dissection of its unique budding mechanism and the design of inhibitors to block it.
Structural basis of membrane budding by the nuclear egress complex of herpesviruses.,Bigalke JM, Heldwein EE EMBO J. 2015 Dec 2;34(23):2921-36. doi: 10.15252/embj.201592359. Epub 2015 Oct, 28. PMID:26511020[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bjerke SL, Cowan JM, Kerr JK, Reynolds AE, Baines JD, Roller RJ. Effects of charged cluster mutations on the function of herpes simplex virus type 1 UL34 protein. J Virol. 2003 Jul;77(13):7601-10. PMID:12805460
- ↑ Reynolds AE, Liang L, Baines JD. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34. J Virol. 2004 Jun;78(11):5564-75. PMID:15140953 doi:http://dx.doi.org/10.1128/JVI.78.11.5564-5575.2004
- ↑ Simpson-Holley M, Baines J, Roller R, Knipe DM. Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late maturation of viral replication compartments to the nuclear periphery. J Virol. 2004 Jun;78(11):5591-600. PMID:15140956 doi:http://dx.doi.org/10.1128/JVI.78.11.5591-5600.2004
- ↑ Bigalke JM, Heldwein EE. Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J. 2015 Dec 2;34(23):2921-36. doi: 10.15252/embj.201592359. Epub 2015 Oct, 28. PMID:26511020 doi:http://dx.doi.org/10.15252/embj.201592359
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