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==Full structure of RYMV P1 protein, derived from crystallographic and NMR data.==
==Full structure of RYMV P1 protein, derived from crystallographic and NMR data.==
<StructureSection load='6xv2' size='340' side='right'caption='[[6xv2]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
<StructureSection load='6xv2' size='340' side='right'caption='[[6xv2]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6xv2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XV2 FirstGlance]. <br>
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XV2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6ty0|6ty0]], [[6ty2|6ty2]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6xv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xv2 OCA], [https://pdbe.org/6xv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xv2 RCSB], [https://www.ebi.ac.uk/pdbsum/6xv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xv2 ProSAT]</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=6xv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xv2 OCA], [https://pdbe.org/6xv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xv2 RCSB], [https://www.ebi.ac.uk/pdbsum/6xv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xv2 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Viruses of the sobemovirus genus are plant viruses, most of which generate very important agricultural and financial losses. Among them, the rice yellow mottle virus (RYMV) is one of the most damaging pathogens devastating rice fields in Africa. RYMV infectivity and propagation rely on its protein P1, identified as a key movement and potential long-distance RNA silencing suppressor. Here we describe P1's complete 3D structure and dynamics obtained by an integrative approach combining X-Ray crystallography and NMR spectroscopy. We show that P1 is organized in two semi-independent and topologically unrelated domains, each harboring an original zinc finger. The two domains exhibit different affinities for zinc and sensitivities to oxidoreduction conditions, making the C-terminal P1 region a potential labile sensor of the plant redox status. An additional level of regulation resides on the capacity of P1 to oligomerize through its N-terminal domain. Coupling P1 structure information with site-directed mutagenesis and plant functional assays, we identified key residues in each zinc domain essential for infectivity and spread in rice tissues. Altogether, our results provide the first complete structure of a sobemoviral P1 movement protein and highlight structural and dynamical properties that may serve RYMV functions to infect and invade its host plant.
A Flexible and Original Architecture of Two Unrelated Zinc Fingers Underlies the Role of the Multitask P1 in RYMV Spread.,Poignavent V, Hoh F, Terral G, Yang Y, Gillet FX, Kim JH, Allemand F, Lacombe E, Brugidou C, Cianferani S, Demene H, Vignols F J Mol Biol. 2022 Aug 30;434(16):167715. doi: 10.1016/j.jmb.2022.167715. Epub 2022, Jul 4. PMID:35798161<ref>PMID:35798161</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xv2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Demene, H]]
[[Category: Demene H]]
[[Category: Gillet, F X]]
[[Category: Gillet FX]]
[[Category: Hoh, F]]
[[Category: Hoh F]]
[[Category: Poignavent, V]]
[[Category: Poignavent V]]
[[Category: Vignols, F]]
[[Category: Vignols F]]
[[Category: Yang, Y]]
[[Category: Yang Y]]
[[Category: Putative rna binding protein]]
[[Category: Silencing suppressor]]
[[Category: Viral protein]]

Latest revision as of 09:09, 19 June 2024

Full structure of RYMV P1 protein, derived from crystallographic and NMR data.Full structure of RYMV P1 protein, derived from crystallographic and NMR data.

Structural highlights

Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT
Drag the structure with the mouse to rotate

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OCA
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