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2mf0

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{{Large structure}}
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==Structural basis of the non-coding RNA RsmZ acting as protein sponge: Conformer L of RsmZ(1-72)/RsmE(dimer) 1to3 complex==
==Structural basis of the non-coding RNA RsmZ acting as protein sponge: Conformer L of RsmZ(1-72)/RsmE(dimer) 1to3 complex==
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<StructureSection load='2mf0' size='340' side='right' caption='[[2mf0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2mf0' size='340' side='right'caption='[[2mf0]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mf0]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Psef5 Psef5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MF0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2mf0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] and [https://en.wikipedia.org/wiki/Pseudomonas_protegens_Pf-5 Pseudomonas protegens Pf-5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MF0 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mf1|2mf1]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rsmE, csrA, PFL_2095 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220664 PSEF5])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf0 OCA], [https://pdbe.org/2mf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mf0 RCSB], [https://www.ebi.ac.uk/pdbsum/2mf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf0 ProSAT]</span></td></tr>
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<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=2mf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf0 OCA], [http://pdbe.org/2mf0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mf0 RCSB], [http://www.ebi.ac.uk/pdbsum/2mf0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf0 ProSAT]</span></td></tr>
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</table>
</table>
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{{Large structure}}
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q4KEY0_PSEF5 Q4KEY0_PSEF5]] Could accelerate the degradation of some genes transcripts potentially through selective RNA binding (By similarity).[HAMAP-Rule:MF_00167][SAAS:SAAS003751_004_007709]
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[https://www.uniprot.org/uniprot/CSRA1_PSEPH CSRA1_PSEPH] A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability (PubMed:17704818, PubMed:23635605). Post-transcriptionally represses the expression of genes controlled by GacA/GacS (PubMed:15601712, PubMed:23635605). Binds the 5' UTR of mRNA; the mRNA binds to the outside edge to each monomer and each dimer could bind the same mRNA twice (PubMed:17704818). Recognizes a (A/U)CANGGANG(U/A) consensus, binds to GGA (part of the Shine-Dalgarno sequence) in the 5' UTR loop, which prevents ribosome binding (PubMed:17704818, PubMed:24561806, PubMed:23635605). Overexpression represses target protein expression; mutating nucleotides in the 5' UTR abolishes repression in vivo (PubMed:17704818, PubMed:23635605). Binds specifically to small RNAs (sRNA) RsmX, RsmZ and RsmY; these sRNAs fold into secondary structures with multiple GGA sequences in loops to which the CsrA proteins bind (PubMed:15601712, PubMed:16286659, PubMed:24828038). Binding to RsmX, RsmY or RsmZ titrates the protein so that it can no longer bind mRNA and repress translation (PubMed:15601712, PubMed:24828038). RsmZ can bind up to 5 CsrA1 (rsmE) dimers; they bind cooperatively to GGA sequences in RsmZ in a defined order (PubMed:24828038, PubMed:24561806). Required for optimal expression and stability of sRNAs RsmX, RsmY and RsmZ (PubMed:15601712, PubMed:16286659). Four CsrA1 dimers maximally protect RsmZ from RNase activity (PubMed:24828038). Deletion of rsmX, rsmY or rsmZ alone has no detectable phenotype, but a double rsmY-rsmZ deletion has a marked decrease in production of secondary metabolites HCN, exoprotease AprA, antifungal agent 2,4-diacetylphloroglucinol and swarming motility, and protects cucumber plants from fungal infection less well than wild-type; the triple sRNA deletion has even stronger loss of these phenotypes (PubMed:16286659).<ref>PMID:15601712</ref> <ref>PMID:16286659</ref> <ref>PMID:17704818</ref> <ref>PMID:23635605</ref> <ref>PMID:24561806</ref> <ref>PMID:24828038</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MicroRNA and protein sequestration by non-coding RNAs (ncRNAs) has recently generated much interest. In the bacterial Csr/Rsm system, which is considered to be the most general global post-transcriptional regulatory system responsible for bacterial virulence, ncRNAs such as CsrB or RsmZ activate translation initiation by sequestering homodimeric CsrA-type proteins from the ribosome-binding site of a subset of messenger RNAs. However, the mechanism of ncRNA-mediated protein sequestration is not understood at the molecular level. Here we show for Pseudomonas fluorescens that RsmE protein dimers assemble sequentially, specifically and cooperatively onto the ncRNA RsmZ within a narrow affinity range. This assembly yields two different native ribonucleoprotein structures. Using a powerful combination of nuclear magnetic resonance and electron paramagnetic resonance spectroscopy we elucidate these 70-kilodalton solution structures, thereby revealing the molecular mechanism of the sequestration process and how RsmE binding protects the ncRNA from RNase E degradation. Overall, our findings suggest that RsmZ is well-tuned to sequester, store and release RsmE and therefore can be viewed as an ideal protein 'sponge'.
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Structural basis of the non-coding RNA RsmZ acting as a protein sponge.,Duss O, Michel E, Yulikov M, Schubert M, Jeschke G, Allain FH Nature. 2014 May 29;509(7502):588-92. doi: 10.1038/nature13271. Epub 2014 May 14. PMID:24828038<ref>PMID:24828038</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mf0" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Psef5]]
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[[Category: Large Structures]]
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[[Category: Allain, F H.T]]
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[[Category: Pseudomonas fluorescens]]
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[[Category: Duss, O]]
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[[Category: Pseudomonas protegens Pf-5]]
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[[Category: Jeschke, G]]
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[[Category: Allain FH-T]]
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[[Category: Michel, E]]
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[[Category: Duss O]]
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[[Category: Schubert, M]]
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[[Category: Jeschke G]]
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[[Category: Yulikov, M]]
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[[Category: Michel E]]
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[[Category: Cooperativity]]
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[[Category: Schubert M]]
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[[Category: Electron paramagnetic resonance]]
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[[Category: Yulikov M]]
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[[Category: Homo-dimeric protein]]
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[[Category: Large solution structure]]
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[[Category: Messenger rna]]
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[[Category: Multiple protein binding site]]
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[[Category: Non-coding rna]]
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[[Category: Protein sequestration]]
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[[Category: Protein sponge]]
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[[Category: Protein/rna]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Ribosome binding site]]
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[[Category: Rna binding protein-rna complex]]
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[[Category: Rnase e cleave site]]
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[[Category: Rnp assembly]]
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[[Category: Translation activation]]
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[[Category: Translation repressor protein]]
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[[Category: Two conformation]]
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Current revision

Structural basis of the non-coding RNA RsmZ acting as protein sponge: Conformer L of RsmZ(1-72)/RsmE(dimer) 1to3 complex

PDB ID 2mf0

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