5lvc: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Aichi virus 1: empty particle== | ==Aichi virus 1: empty particle== | ||
< | <SX load='5lvc' size='340' side='right' viewer='molstar' caption='[[5lvc]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lvc]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5lvc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aichivirus_A Aichivirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LVC FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2Å</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=5lvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvc OCA], [https://pdbe.org/5lvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lvc RCSB], [https://www.ebi.ac.uk/pdbsum/5lvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/POLG_AIVA8 POLG_AIVA8] Required for viral RNA replication and viral RNA encapsidation (PubMed:14512530). Does not have any proteolytic activity (PubMed:14512530).<ref>PMID:14512530</ref> Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (PubMed:27681122, PubMed:27595320). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:27595320).<ref>PMID:27595320</ref> <ref>PMID:27681122</ref> Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (PubMed:27681122, PubMed:27595320). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:27595320).<ref>PMID:27595320</ref> <ref>PMID:27681122</ref> Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (PubMed:27681122, PubMed:27595320). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:27595320).<ref>PMID:27595320</ref> <ref>PMID:27681122</ref> Required for viral RNA replication (PubMed:18653460). Does not have any proteolytic activity (PubMed:18653460).<ref>PMID:18653460</ref> Affects membrane integrity and causes an increase in membrane permeability. Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[UniProtKB:P03300] Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (PubMed:22124328, PubMed:24672044, PubMed:27989622, PubMed:30755512, PubMed:22258260). Stimulates the enzymatic activity of PI4KB, this activation is sensitized by ACBD3 (PubMed:24672044, PubMed:27989622).<ref>PMID:22124328</ref> <ref>PMID:22258260</ref> <ref>PMID:24672044</ref> <ref>PMID:27989622</ref> <ref>PMID:30755512</ref> Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.[UniProtKB:P03304] Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease (By similarity).[UniProtKB:P03304][UniProtKB:P12296] Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity).[UniProtKB:P12296] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 21: | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</ | </SX> | ||
[[Category: | [[Category: Aichivirus A]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fuzik | [[Category: Fuzik T]] | ||
[[Category: Lindberg | [[Category: Lindberg AM]] | ||
[[Category: Palkova | [[Category: Palkova L]] | ||
[[Category: Plevka | [[Category: Plevka P]] | ||
[[Category: Sabin | [[Category: Sabin C]] | ||
[[Category: Skubnik | [[Category: Skubnik K]] | ||