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| | <StructureSection load='5doe' size='340' side='right'caption='[[5doe]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5doe' size='340' side='right'caption='[[5doe]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5doe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hcmva Hcmva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DOE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5doe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_AD169 Human herpesvirus 5 strain AD169]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DOE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dob|5dob]], [[5doc|5doc]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UL53 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10360 HCMVA])</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=5doe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5doe OCA], [https://pdbe.org/5doe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5doe RCSB], [https://www.ebi.ac.uk/pdbsum/5doe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5doe ProSAT]</span></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=5doe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5doe OCA], [http://pdbe.org/5doe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5doe RCSB], [http://www.ebi.ac.uk/pdbsum/5doe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5doe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UL53_HCMVA UL53_HCMVA]] 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, UL53/UL50 complex induces capsids budding and envelopment into the perinuclear space. Then UL53/UL50 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 (By similarity). | + | [https://www.uniprot.org/uniprot/NEC1_HCMVA NEC1_HCMVA] 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_04023]<ref>PMID:25339763</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: Hcmva]] | + | [[Category: Human herpesvirus 5 strain AD169]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Filman, D J]] | + | [[Category: El Omari K]] |
| - | [[Category: Hogle, J M]]
| + | [[Category: Filman DJ]] |
| - | [[Category: Lye, M F]]
| + | [[Category: Hogle JM]] |
| - | [[Category: Omari, K El]]
| + | [[Category: Lye MF]] |
| - | [[Category: Bergerat fold]] | + | |
| - | [[Category: Dna binding protein]] | + | |
| - | [[Category: Zinc finger]] | + | |
| Structural highlights
Function
NEC1_HCMVA 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_04023][1]
Publication Abstract from PubMed
Herpesvirus nucleocapsids escape from the nucleus in a process orchestrated by a highly conserved, viral nuclear egress complex. In human cytomegalovirus, the complex consists of two proteins, UL50 and UL53. We solved structures of versions of UL53 and the complex by X-ray crystallography. The UL53 structures, determined at 1.93 and 3.0 A resolution, contained unexpected features including a Bergerat fold resembling that found in certain nucleotide-binding proteins, and a Cys3His zinc finger. Substitutions of zinc-coordinating residues decreased UL50-UL53 co-localization in transfected cells, and, when incorporated into the HCMV genome, ablated viral replication. The structure of the complex, determined at 2.47 A resolution, revealed a mechanism of heterodimerization in which UL50 clamps onto helices of UL53 like a vise. Substitutions of particular residues on the interaction interface disrupted UL50-UL53 co-localization in transfected cells and abolished virus production. The structures and the identification of contacts can be harnessed toward the rational design of novel and highly specific antiviral drugs and will aid in the detailed understanding of nuclear egress.
Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex.,Lye MF, Sharma M, El Omari K, Filman DJ, Schuermann JP, Hogle JM, Coen DM EMBO J. 2015 Oct 28. pii: e201592651. PMID:26511021[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sharma M, Bender BJ, Kamil JP, Lye MF, Pesola JM, Reim NI, Hogle JM, Coen DM. Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex. J Virol. 2015 Jan;89(1):523-34. PMID:25339763 doi:10.1128/JVI.02426-14
- ↑ Lye MF, Sharma M, El Omari K, Filman DJ, Schuermann JP, Hogle JM, Coen DM. Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex. EMBO J. 2015 Oct 28. pii: e201592651. PMID:26511021 doi:http://dx.doi.org/10.15252/embj.201592651
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