View source for 7zv1


==Crystal Structure of Aichivirus A 2A protein L64M, L109M mutant==
<StructureSection load='7zv1' size='340' side='right'caption='[[7zv1]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zv1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aichi_virus_A846/88 Aichi virus A846/88]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZV1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</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=7zv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zv1 OCA], [https://pdbe.org/7zv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zv1 RCSB], [https://www.ebi.ac.uk/pdbsum/7zv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zv1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POLG_AIVA8 POLG_AIVA8] Inhibits the integrated stress response (ISR) in the infected cell by preventing the sequestration of eIF2B by phosphorylated EIF2S1/eIF-2alpha (PubMed:32690955). Stress granule formation in response to EIF2S1/eIF-2alpha phosphorylation is thus inhibited, which allows protein synthesis and viral replication (PubMed:32690955). Does not have any proteolytic activity (PubMed:14512530). Required for viral RNA replication and viral RNA encapsidation (PubMed:14512530).<ref>PMID:14512530</ref> <ref>PMID:32690955</ref>   Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (PubMed:27595320, PubMed:27681122). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27595320, PubMed:27681122). 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:27595320, PubMed:27681122). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27595320, PubMed:27681122). 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:27595320, PubMed:27681122). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27595320, PubMed:27681122). 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:22258260, PubMed:24672044, PubMed:27989622, PubMed:30755512). 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]
== References ==
<references/>
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</StructureSection>
[[Category: Aichi virus A846/88]]
[[Category: Large Structures]]
[[Category: Perrakis A]]
[[Category: Von Castelmur E]]