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| | ==The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.== | | ==The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.== |
| - | <StructureSection load='3k7b' size='340' side='right' caption='[[3k7b]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3k7b' size='340' side='right'caption='[[3k7b]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k7b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus_wr Vaccinia virus wr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K7B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k7b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_WR Vaccinia virus WR]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K7B FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A33R, SALL3R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 Vaccinia virus WR])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3k7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k7b RCSB], [http://www.ebi.ac.uk/pdbsum/3k7b PDBsum]</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=3k7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7b OCA], [https://pdbe.org/3k7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k7b RCSB], [https://www.ebi.ac.uk/pdbsum/3k7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k7b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VA33_VACCW VA33_VACCW]] Coordinates the incorporation of A36 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails. Therefore plays an essential role in efficient cell-to-cell spread of viral particles.<ref>PMID:9557708</ref> <ref>PMID:11119600</ref> <ref>PMID:14581563</ref> | + | [https://www.uniprot.org/uniprot/PG161_VACCW PG161_VACCW] Forms a complex with OPG162 and OPG190 to coordinate the incorporation of OPG164 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails (PubMed:11119600, PubMed:23255618, PubMed:31941777). Therefore plays an essential role in efficient cell-to-cell spread of viral particles.<ref>PMID:11119600</ref> <ref>PMID:14581563</ref> <ref>PMID:23255618</ref> <ref>PMID:31941777</ref> <ref>PMID:9557708</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/3k7b_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/3k7b_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k7b ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3k7b" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vaccinia virus wr]] | + | [[Category: Large Structures]] |
| - | [[Category: Garboczi, D N]] | + | [[Category: Vaccinia virus WR]] |
| - | [[Category: Su, H P]] | + | [[Category: Garboczi DN]] |
| - | [[Category: C-type lectin-like domain]] | + | [[Category: Su HP]] |
| - | [[Category: Eev]]
| + | |
| - | [[Category: Ev]]
| + | |
| - | [[Category: Homodimer]]
| + | |
| - | [[Category: Poxvirus]]
| + | |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
PG161_VACCW Forms a complex with OPG162 and OPG190 to coordinate the incorporation of OPG164 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails (PubMed:11119600, PubMed:23255618, PubMed:31941777). Therefore plays an essential role in efficient cell-to-cell spread of viral particles.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (CTLDs) that occur as dimers in A33 crystals with five different crystal lattices. Comparison of the A33 dimer models shows that the A33 monomers have a degree of flexibility in position within the dimer. Structural comparisons show that the A33 monomer is a close match to the Link module class of CTLDs but that the A33 dimer is most similar to the natural killer (NK)-cell receptor class of CTLDs. Structural data on Link modules and NK-cell receptor-ligand complexes suggest a surface of A33 that could interact with viral or host ligands. The dimer interface is well conserved in all known A33 sequences, indicating an important role for the A33 dimer. The structure indicates how previously described A33 mutations disrupt protein folding and locates the positions of N-linked glycosylations and the epitope of a protective antibody.
The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.,Su HP, Singh K, Gittis AG, Garboczi DN J Virol. 2010 Mar;84(5):2502-10. Epub 2009 Dec 23. PMID:20032175[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wolffe EJ, Weisberg AS, Moss B. The vaccinia virus A33R protein provides a chaperone function for viral membrane localization and tyrosine phosphorylation of the A36R protein. J Virol. 2001 Jan;75(1):303-10. PMID:11119600 doi:http://dx.doi.org/10.1128/JVI.75.1.303-310.2001
- ↑ Katz E, Ward BM, Weisberg AS, Moss B. Mutations in the vaccinia virus A33R and B5R envelope proteins that enhance release of extracellular virions and eliminate formation of actin-containing microvilli without preventing tyrosine phosphorylation of the A36R protein. J Virol. 2003 Nov;77(22):12266-75. PMID:14581563
- ↑ Breiman A, Carpentier DCJ, Ewles HA, Smith GL. Transport and stability of the vaccinia virus A34 protein is affected by the A33 protein. J Gen Virol. 2013 Apr;94(Pt 4):720-725. PMID:23255618 doi:10.1099/vir.0.049486-0
- ↑ Monticelli SR, Earley AK, Stone R, Norbury CC, Ward BM. Vaccinia Virus Glycoproteins A33, A34, and B5 Form a Complex for Efficient Endoplasmic Reticulum to trans-Golgi Network Transport. J Virol. 2020 Mar 17;94(7):e02155-19. PMID:31941777 doi:10.1128/JVI.02155-19
- ↑ Roper RL, Wolffe EJ, Weisberg A, Moss B. The envelope protein encoded by the A33R gene is required for formation of actin-containing microvilli and efficient cell-to-cell spread of vaccinia virus. J Virol. 1998 May;72(5):4192-204. PMID:9557708
- ↑ Su HP, Singh K, Gittis AG, Garboczi DN. The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains. J Virol. 2010 Mar;84(5):2502-10. Epub 2009 Dec 23. PMID:20032175 doi:10.1128/JVI.02247-09
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