6o3v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6o3v is ON HOLD until Paper Publication
+
==Crystal structure for RVA-VP3==
-
 
+
<StructureSection load='6o3v' size='340' side='right'caption='[[6o3v]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[6o3v]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O3V FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
[[Category: Unreleased Structures]]
+
<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=6o3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3v OCA], [http://pdbe.org/6o3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o3v RCSB], [http://www.ebi.ac.uk/pdbsum/6o3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3v ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/Q1WK45_9REOV Q1WK45_9REOV]] Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'-oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated.[HAMAP-Rule:MF_04128] Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not.[HAMAP-Rule:MF_04128]
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Hu, L]]
 +
[[Category: Kumar, D]]
 +
[[Category: Prasad, V]]
 +
[[Category: Wang, Z]]
 +
[[Category: Yu, X]]
 +
[[Category: Capping enzyme]]
 +
[[Category: Guanylyl transferase]]
 +
[[Category: Methyl transferase]]
 +
[[Category: Pde]]
 +
[[Category: Rotavirus]]
 +
[[Category: Rtpase]]
 +
[[Category: Structural protein]]
 +
[[Category: Vp3]]

Revision as of 06:43, 4 March 2020

Crystal structure for RVA-VP3

PDB ID 6o3v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools