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==Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization==
==Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization==
<StructureSection load='1lj2' size='340' side='right' caption='[[1lj2]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='1lj2' size='340' side='right'caption='[[1lj2]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lj2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Simian_11_rotavirus Simian 11 rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LJ2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lj2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Simian_rotavirus_A/SA11 Simian rotavirus A/SA11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJ2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU:GOLD+ION'>AU</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]] 2.38&#8491;</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=1lj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj2 OCA], [http://pdbe.org/1lj2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lj2 RCSB], [http://www.ebi.ac.uk/pdbsum/1lj2 PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</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=1lj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj2 OCA], [https://pdbe.org/1lj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lj2 RCSB], [https://www.ebi.ac.uk/pdbsum/1lj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lj2 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/IF4G1_HUMAN IF4G1_HUMAN]] Defects in EIF4G1 are the cause of Parkinson disease type 18 (PARK18) [MIM:[http://omim.org/entry/614251 614251]]. An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.<ref>PMID:21907011</ref> 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NSP3_ROTS1 NSP3_ROTS1]] Involved in the shutoff of host protein synthesis. It is unclear whether it is required for the translation of viral mRNAs as well. Functions similarly to, and competes with the cellular poly(A)-binding protein PABPC1. Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs and allows circularization of viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with the eukaryotic translation initiation factor eIF4G, using the same region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the translation of cellular poly(A) mRNAs. Also responsible for the nuclear relocalization of PABPC1 upon rotavirus infection (By similarity). [[http://www.uniprot.org/uniprot/IF4G1_HUMAN IF4G1_HUMAN]] Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.  
[https://www.uniprot.org/uniprot/NSP3_ROTS1 NSP3_ROTS1] Involved in the shutoff of host protein synthesis. It is unclear whether it is required for the translation of viral mRNAs as well. Functions similarly to, and competes with the cellular poly(A)-binding protein PABPC1. Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs and allows circularization of viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with the eukaryotic translation initiation factor eIF4G, using the same region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the translation of cellular poly(A) mRNAs. Also responsible for the nuclear relocalization of PABPC1 upon rotavirus infection (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lj/1lj2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lj/1lj2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lj2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.
Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization.,Groft CM, Burley SK Mol Cell. 2002 Jun;9(6):1273-83. PMID:12086624<ref>PMID:12086624</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lj2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Nonstructural protein|Nonstructural protein]]
*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Simian 11 rotavirus]]
[[Category: Homo sapiens]]
[[Category: Burley, S K]]
[[Category: Large Structures]]
[[Category: Groft, C M]]
[[Category: Simian rotavirus A/SA11]]
[[Category: Closed loop]]
[[Category: Burley SK]]
[[Category: Coiled coil]]
[[Category: Groft CM]]
[[Category: Eif4g]]
[[Category: Homodimer]]
[[Category: Mrna]]
[[Category: Nsp3]]
[[Category: Rotavirus]]
[[Category: Translation]]
[[Category: Viral protein- translation complex]]

Latest revision as of 10:33, 14 February 2024

Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularizationRecognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization

Structural highlights

1lj2 is a 4 chain structure with sequence from Homo sapiens and Simian rotavirus A/SA11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.38Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NSP3_ROTS1 Involved in the shutoff of host protein synthesis. It is unclear whether it is required for the translation of viral mRNAs as well. Functions similarly to, and competes with the cellular poly(A)-binding protein PABPC1. Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs and allows circularization of viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with the eukaryotic translation initiation factor eIF4G, using the same region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the translation of cellular poly(A) mRNAs. Also responsible for the nuclear relocalization of PABPC1 upon rotavirus infection (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1lj2, resolution 2.38Å

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