6w2t - Revision history

OCA at 09:30, 20 March 2024

OCA — Wed, 20 Mar 2024 09:30:09 GMT

←Older revision		Revision as of 09:30, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='6w2t' size='340' side='right'caption='[[6w2t]], [[Resolution\|resolution]] 3.36Å' scene=''>		<StructureSection load='6w2t' size='340' side='right'caption='[[6w2t]], [[Resolution\|resolution]] 3.36Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6w2t]] is a 44 chain structure with sequence from [~~http://en.wikipedia.org/wiki/ ] and [http~~://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W2T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6W2T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6w2t]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W2T FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~, ~~<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">Electron Microscopy, [[Resolution\|Resolution]] 3.36Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[6w2s\|6w2s]]~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6w2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w2t OCA], [~~http~~://pdbe.org/6w2t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6w2t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6w2t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6w2t 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=6w2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w2t OCA], [https://pdbe.org/6w2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w2t RCSB], [https://www.ebi.ac.uk/pdbsum/6w2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w2t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/G1TWL4_RABIT G1TWL4_RABIT]] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA.[HAMAP-Rule:MF_03016] [[http://www.uniprot.org/uniprot/G1SMZ5_RABIT G1SMZ5_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03000] [[http://www.uniprot.org/uniprot/G1SUC8_RABIT G1SUC8_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins.[HAMAP-Rule:MF_03004] [[http://www.uniprot.org/uniprot/EIF3D_NASVI EIF3D_NASVI]] mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.[HAMAP-Rule:MF_03003] [[http://www.uniprot.org/uniprot/G1SLW8_RABIT G1SLW8_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03012] [[http://www.uniprot.org/uniprot/G1SLC2_RABIT G1SLC2_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.[HAMAP-Rule:MF_03005] [[http://www.uniprot.org/uniprot/G1SS70_RABIT G1SS70_RABIT]] May play a role during erythropoiesis through regulation of transcription factor DDIT3.[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/G1U971_RABIT G1U971_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03002] [[http://www.uniprot.org/uniprot/G1T3L2_RABIT G1T3L2_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03010] [[http://www.uniprot.org/uniprot/G1ST95_RABIT G1ST95_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03007]	+	[https://www.uniprot.org/uniprot/G1U971_RABIT G1U971_RABIT] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03002]
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Taking control of the cellular apparatus for protein production is a requirement for virus progression. To ensure this control, diverse strategies of cellular mimicry and/or ribosome hijacking evolved. The initiation stage of translation is specially targeted as it involves multiple steps and the engagement of numerous initiation factors. The use of structured RNA sequences, called Internal Ribosomal Entry Sites (IRES) in viral RNAs is a widespread strategy for the exploitation of eukaryotic initiation. Using a combination of electron cryo-microscopy (cryo-EM) and reconstituted translation initiation assays with native components, we characterized how a novel IRES at the 5'-UTR of a viral RNA assembles a functional initiation complex via an uAUG intermediate. The IRES features a novel extended, multi-domain architecture, circling the 40S head. The structures and accompanying functional data, illustrate the importance of 5'-UTR regions in translation regulation and underline the relevance of the untapped diversity of viral IRESs.	+

-	A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S complex via an uAUG intermediate.,Neupane R, Pisareva VP, Rodriguez CF, Pisarev AV, Fernandez IS Elife. 2020 Apr 14;9. pii: 54575. doi: 10.7554/eLife.54575. PMID:32286223<ref>PMID:32286223</ref>	+	==See Also==
-		+	*[[Ribosome 3D structures\|Ribosome 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+	*[[3D sructureseceptor for activated protein kinase C 1\|3D sructureseceptor for activated protein kinase C 1]]
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 6w2t" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	[[Category: Fernandez~~, I S~~]]	+	[[Category: Fernandez IS]]
-	[[Category: Neupane, R]]	+	[[Category: Neupane R]]
-	[[Category: Pisarev, A]]	+	[[Category: Pisarev A]]
-	[[Category: Pisareva, V]]	+	[[Category: Pisareva V]]
-	[[Category: Rodriguez~~, C F]]~~	+	[[Category: Rodriguez CF]]
-	~~[[Category: Crpv 5'-utr ire]]~~	+
-	~~[[Category: Internal ribosome entry site]]~~	+
-	~~[[Category: Ribosome~~]]	+

OCA at 07:18, 29 April 2020

OCA — Wed, 29 Apr 2020 07:18:11 GMT

←Older revision		Revision as of 07:18, 29 April 2020
Line 1:		Line 1:

	==Structure of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit in the closed state (Class 2)==		==Structure of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit in the closed state (Class 2)==
-	<StructureSection load='6w2t' size='340' side='right'caption='[[6w2t]]' scene=''>	+	<StructureSection load='6w2t' size='340' side='right'caption='[[6w2t]], [[Resolution\|resolution]] 3.36Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W2T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W2T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6w2t]] is a 44 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W2T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W2T FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w2t OCA], [http://pdbe.org/6w2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w2t RCSB], [http://www.ebi.ac.uk/pdbsum/6w2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w2t ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6w2s\|6w2s]]</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w2t OCA], [http://pdbe.org/6w2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w2t RCSB], [http://www.ebi.ac.uk/pdbsum/6w2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w2t ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/G1TWL4_RABIT G1TWL4_RABIT]] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA.[HAMAP-Rule:MF_03016] [[http://www.uniprot.org/uniprot/G1SMZ5_RABIT G1SMZ5_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03000] [[http://www.uniprot.org/uniprot/G1SUC8_RABIT G1SUC8_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins.[HAMAP-Rule:MF_03004] [[http://www.uniprot.org/uniprot/EIF3D_NASVI EIF3D_NASVI]] mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.[HAMAP-Rule:MF_03003] [[http://www.uniprot.org/uniprot/G1SLW8_RABIT G1SLW8_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03012] [[http://www.uniprot.org/uniprot/G1SLC2_RABIT G1SLC2_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.[HAMAP-Rule:MF_03005] [[http://www.uniprot.org/uniprot/G1SS70_RABIT G1SS70_RABIT]] May play a role during erythropoiesis through regulation of transcription factor DDIT3.[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/G1U971_RABIT G1U971_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03002] [[http://www.uniprot.org/uniprot/G1T3L2_RABIT G1T3L2_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03010] [[http://www.uniprot.org/uniprot/G1ST95_RABIT G1ST95_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03007]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Taking control of the cellular apparatus for protein production is a requirement for virus progression. To ensure this control, diverse strategies of cellular mimicry and/or ribosome hijacking evolved. The initiation stage of translation is specially targeted as it involves multiple steps and the engagement of numerous initiation factors. The use of structured RNA sequences, called Internal Ribosomal Entry Sites (IRES) in viral RNAs is a widespread strategy for the exploitation of eukaryotic initiation. Using a combination of electron cryo-microscopy (cryo-EM) and reconstituted translation initiation assays with native components, we characterized how a novel IRES at the 5'-UTR of a viral RNA assembles a functional initiation complex via an uAUG intermediate. The IRES features a novel extended, multi-domain architecture, circling the 40S head. The structures and accompanying functional data, illustrate the importance of 5'-UTR regions in translation regulation and underline the relevance of the untapped diversity of viral IRESs.
		+
		+	A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S complex via an uAUG intermediate.,Neupane R, Pisareva VP, Rodriguez CF, Pisarev AV, Fernandez IS Elife. 2020 Apr 14;9. pii: 54575. doi: 10.7554/eLife.54575. PMID:32286223<ref>PMID:32286223</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6w2t" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fernandez IS]]	+	[[Category: Oryctolagus cuniculus]]
-	[[Category: Neupane R]]	+	[[Category: Fernandez, I S]]
-	[[Category: Pisarev A]]	+	[[Category: Neupane, R]]
-	[[Category: Pisareva V]]	+	[[Category: Pisarev, A]]
-	[[Category: Rodriguez CF]]	+	[[Category: Pisareva, V]]
		+	[[Category: Rodriguez, C F]]
		+	[[Category: Crpv 5'-utr ire]]
		+	[[Category: Internal ribosome entry site]]
		+	[[Category: Ribosome]]

OCA at 05:47, 22 April 2020

OCA — Wed, 22 Apr 2020 05:47:58 GMT

←Older revision		Revision as of 05:47, 22 April 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 6w2t is ON HOLD~~	+	==Structure of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit in the closed state (Class 2)==
-		+	<StructureSection load='6w2t' size='340' side='right'caption='[[6w2t]]' scene=''>
-	~~Authors: Neupane, R., Pisareva, V., Rodriguez, C.F., Pisarev, A., Fernandez, I.S.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W2T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W2T FirstGlance]. <br>
-	~~Description:~~ Structure of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit in the closed state (Class 2)	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w2t OCA], [http://pdbe.org/6w2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w2t RCSB], [http://www.ebi.ac.uk/pdbsum/6w2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w2t ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Rodriguez~~, C.F]]	+	__TOC__
-	[[Category: ~~Pisarev, A~~]]	+	</StructureSection>
-	[[Category: Fernandez~~, I.S~~]]	+	[[Category: Large Structures]]
-	[[Category: Neupane, R]]	+	[[Category: Fernandez IS]]
-	[[Category: Pisareva, V]]	+	[[Category: Neupane R]]
		+	[[Category: Pisarev A]]
		+	[[Category: Pisareva V]]
		+	[[Category: Rodriguez CF]]

OCA: Protected "6w2t" [edit=sysop:move=sysop]

OCA — Wed, 18 Mar 2020 08:30:56 GMT

Protected "6w2t" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:30, 18 March 2020

OCA: New page: '''Unreleased structure''' The entry 6w2t is ON HOLD Authors: Neupane, R., Pisareva, V., Rodriguez, C.F., Pisarev, A., Fernandez, I.S. Description: Structure of the Cricket Paralysis V...

OCA — Wed, 18 Mar 2020 08:30:54 GMT

New page: '''Unreleased structure''' The entry 6w2t is ON HOLD Authors: Neupane, R., Pisareva, V., Rodriguez, C.F., Pisarev, A., Fernandez, I.S. Description: Structure of the Cricket Paralysis V...

New page

'''Unreleased structure'''

The entry 6w2t is ON HOLD

Authors: Neupane, R., Pisareva, V., Rodriguez, C.F., Pisarev, A., Fernandez, I.S.

Description: Structure of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit in the closed state (Class 2)
[[Category: Unreleased Structures]]
[[Category: Rodriguez, C.F]]
[[Category: Pisarev, A]]
[[Category: Fernandez, I.S]]
[[Category: Neupane, R]]
[[Category: Pisareva, V]]