8ago: Difference between revisions

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'''Unreleased structure'''


The entry 8ago is ON HOLD  until Paper Publication
==BK Polyomavirus VP1 mutant E73Q==
 
<StructureSection load='8ago' size='340' side='right'caption='[[8ago]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
Authors: Sorin, M.N., Di Maio, A., Silva, L.M., Ebert, D., Delannoy, C., Nguyen, N.-K., Guerardel, Y., Chai, W., Halary, F., Renaudin-Autain, K., Liu, Y., Bressollette-Bodin, C., Stehle, T., McIlroy, D.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8ago]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_polyomavirus_1 Human polyomavirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AGO FirstGlance]. <br>
Description: BK Polyomavirus VP1 mutant E73Q
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.853&#8491;</td></tr>
[[Category: Unreleased Structures]]
<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=GOL:GLYCEROL'>GOL</scene></td></tr>
[[Category: Chai, W]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ago FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ago OCA], [https://pdbe.org/8ago PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ago RCSB], [https://www.ebi.ac.uk/pdbsum/8ago PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ago ProSAT]</span></td></tr>
[[Category: Guerardel, Y]]
</table>
[[Category: Renaudin-Autain, K]]
== Function ==
[[Category: Mcilroy, D]]
[https://www.uniprot.org/uniprot/VP1_POVBK VP1_POVBK] Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA (By similarity).<ref>PMID:15479799</ref> <ref>PMID:16415013</ref>
[[Category: Delannoy, C]]
== References ==
[[Category: Halary, F]]
<references/>
[[Category: Ebert, D]]
__TOC__
[[Category: Liu, Y]]
</StructureSection>
[[Category: Silva, L.M]]
[[Category: Human polyomavirus 1]]
[[Category: Bressollette-Bodin, C]]
[[Category: Large Structures]]
[[Category: Sorin, M.N]]
[[Category: Bressollette-Bodin C]]
[[Category: Nguyen, N.-K]]
[[Category: Chai W]]
[[Category: Di Maio, A]]
[[Category: Delannoy C]]
[[Category: Stehle, T]]
[[Category: Di Maio A]]
[[Category: Ebert D]]
[[Category: Guerardel Y]]
[[Category: Halary F]]
[[Category: Liu Y]]
[[Category: McIlroy D]]
[[Category: Nguyen N-K]]
[[Category: Renaudin-Autain K]]
[[Category: Silva LM]]
[[Category: Sorin MN]]
[[Category: Stehle T]]

Latest revision as of 11:11, 7 February 2024

BK Polyomavirus VP1 mutant E73QBK Polyomavirus VP1 mutant E73Q

Structural highlights

8ago is a 5 chain structure with sequence from Human polyomavirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.853Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VP1_POVBK Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA (By similarity).[1] [2]

References

  1. Eash S, Querbes W, Atwood WJ. Infection of vero cells by BK virus is dependent on caveolae. J Virol. 2004 Nov;78(21):11583-90. PMID:15479799 doi:http://dx.doi.org/10.1128/JVI.78.21.11583-11590.2004
  2. Low JA, Magnuson B, Tsai B, Imperiale MJ. Identification of gangliosides GD1b and GT1b as receptors for BK virus. J Virol. 2006 Feb;80(3):1361-6. PMID:16415013 doi:http://dx.doi.org/80/3/1361

8ago, resolution 1.85Å

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