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==Crystal structure of tobacco vein mottling virus protease==
==Crystal structure of tobacco vein mottling virus protease==
<StructureSection load='3mmg' size='340' side='right' caption='[[3mmg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3mmg' size='340' side='right'caption='[[3mmg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mmg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Tobacco_vein_mottling_virus Tobacco vein mottling virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MMG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mmg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_vein_mottling_virus Tobacco vein mottling virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MMG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">protease ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12228 Tobacco vein mottling virus])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></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=3mmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mmg RCSB], [http://www.ebi.ac.uk/pdbsum/3mmg PDBsum]</span></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=3mmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmg OCA], [https://pdbe.org/3mmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mmg RCSB], [https://www.ebi.ac.uk/pdbsum/3mmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mmg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POLG_TVMV POLG_TVMV] Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.[UniProtKB:P04517]  Has helicase activity. It may be involved in replication.  Indispensable for virus replication.[UniProtKB:P13529]  Indispensable for virus replication.<ref>PMID:19906931</ref>  Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity).[UniProtKB:P18247]  Has RNA-binding and proteolytic activities.[UniProtKB:P04517]  An RNA-dependent RNA polymerase that plays an essential role in the virus replication.  Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.[UniProtKB:P04517]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3mmg" style="background-color:#fffaf0;"></div>
==See Also==
*[[Tobacco Etch Virus (TEV) Protease|Tobacco Etch Virus (TEV) Protease]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Tobacco vein mottling virus]]
[[Category: Tobacco vein mottling virus]]
[[Category: Austin, B P]]
[[Category: Austin BP]]
[[Category: Ping, S]]
[[Category: Ping S]]
[[Category: Tozser, J]]
[[Category: Tozser J]]
[[Category: Waugh, D S]]
[[Category: Waugh DS]]
[[Category: 3c-type protease]]
[[Category: Hydrolase]]
[[Category: Tev]]
[[Category: Tvmv]]
[[Category: Viral protein]]
Retrieved from "https://proteopedia.org/3mmg"