6a9s
From Proteopedia
(Difference between revisions)
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<StructureSection load='6a9s' size='340' side='right'caption='[[6a9s]], [[Resolution|resolution]] 1.18Å' scene=''> | <StructureSection load='6a9s' size='340' side='right'caption='[[6a9s]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6a9s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A9S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6a9s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccw Vaccw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A9S FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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> | <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> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VACWR149, A26L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW])</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=6a9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9s OCA], [http://pdbe.org/6a9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9s RCSB], [http://www.ebi.ac.uk/pdbsum/6a9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9s 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=6a9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9s OCA], [http://pdbe.org/6a9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9s RCSB], [http://www.ebi.ac.uk/pdbsum/6a9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A26_VACCW A26_VACCW]] Plays a role in bridging the mature virion with structural protein A25. Presence of protein A26 in the virion structurally prevents direct virus-cell fusion mechanism.<ref>PMID:20538855</ref> | [[http://www.uniprot.org/uniprot/A26_VACCW A26_VACCW]] Plays a role in bridging the mature virion with structural protein A25. Presence of protein A26 in the virion structurally prevents direct virus-cell fusion mechanism.<ref>PMID:20538855</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Vaccinia mature virus requires A26 envelope protein to mediate acid-dependent endocytosis into HeLa cells in which we hypothesized that A26 protein functions as an acid-sensitive membrane fusion suppressor. Here, we provide evidence showing that N-terminal domain (aa1-75) of A26 protein is an acid-sensitive region that regulates membrane fusion. Crystal structure of A26 protein revealed that His48 and His53 are in close contact with Lys47, Arg57, His314 and Arg312, suggesting that at low pH these His-cation pairs could initiate conformational changes through protonation of His48 and His53 and subsequent electrostatic repulsion. All the A26 mutant mature viruses that interrupted His-cation pair interactions of His48 and His 53 indeed have lost virion infectivity. Isolation of revertant viruses revealed that second site mutations caused frame shifts and premature termination of A26 protein such that reverent viruses regained cell entry through plasma membrane fusion. Together, we conclude that viral A26 protein functions as an acid-sensitive fusion suppressor during vaccinia mature virus endocytosis. | ||
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| + | Vaccinia viral A26 protein is a fusion suppressor of mature virus and triggers membrane fusion through conformational change at low pH.,Chang HW, Yang CH, Luo YC, Su BG, Cheng HY, Tung SY, Carillo KJD, Liao YT, Tzou DM, Wang HC, Chang W PLoS Pathog. 2019 Jun 20;15(6):e1007826. doi: 10.1371/journal.ppat.1007826., eCollection 2019 Jun. PMID:31220181<ref>PMID:31220181</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6a9s" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Vaccw]] | ||
[[Category: Chang, W]] | [[Category: Chang, W]] | ||
[[Category: Ko, T Z]] | [[Category: Ko, T Z]] | ||
Revision as of 06:15, 10 July 2019
The crystal structure of vaccinia virus A26 (residues 1-397)
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Categories: Large Structures | Vaccw | Chang, W | Ko, T Z | Liao, Y T | Luo, Y C | Wang, H C | Acid sensitive | Vaccinia virus | Viral protein | Virus entry
