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| - | [[Image:1q5x.jpg|left|200px]]<br /><applet load="1q5x" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1q5x, resolution 2.0Å" /> | |
| - | '''Structure of OF RRAA (MENG), a protein inhibitor of RNA processing'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Structure of OF RRAA (MENG), a protein inhibitor of RNA processing== |
| - | The Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing in vivo and in vitro. Here, we report the 2.0A X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12A in diameter. Based on earlier sequence analysis, RraA had been identified as a putative S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the E.coli RraA exhibits an ancient relationship to a family of aldolases.
| + | <StructureSection load='1q5x' size='340' side='right'caption='[[1q5x]], [[Resolution|resolution]] 2.00Å' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <table><tr><td colspan='2'>[[1q5x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5X FirstGlance]. <br> |
| - | 1Q5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5X OCA].
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=1q5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5x OCA], [https://pdbe.org/1q5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q5x RCSB], [https://www.ebi.ac.uk/pdbsum/1q5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q5x ProSAT]</span></td></tr> |
| - | ==Reference== | + | </table> |
| - | The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing., Monzingo AF, Gao J, Qiu J, Georgiou G, Robertus JD, J Mol Biol. 2003 Oct 3;332(5):1015-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14499605 14499605]
| + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RRAA_ECOLI RRAA_ECOLI] Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.<ref>PMID:13678585</ref> <ref>PMID:16725107</ref> <ref>PMID:16771842</ref> <ref>PMID:18510556</ref> <ref>PMID:20106955</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q5/1q5x_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </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/main_output.php?pdb_ID=1q5x ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Gao, J.]] | + | [[Category: Gao J]] |
| - | [[Category: Georgiou, G.]] | + | [[Category: Georgiou G]] |
| - | [[Category: Monzingo, A F.]] | + | [[Category: Monzingo AF]] |
| - | [[Category: Qiu, J.]] | + | [[Category: Qiu J]] |
| - | [[Category: Robertus, J D.]] | + | [[Category: Robertus JD]] |
| - | [[Category: 3-layer sandwich]]
| + | |
| - | [[Category: alpha-beta structure]]
| + | |
| - | [[Category: antiparallel beta sheet]]
| + | |
| - | [[Category: parallel beta sheet]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:16 2008''
| + | |
| Structural highlights
Function
RRAA_ECOLI Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Lee K, Zhan X, Gao J, Qiu J, Feng Y, Meganathan R, Cohen SN, Georgiou G. RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell. 2003 Sep 5;114(5):623-34. PMID:13678585
- ↑ Yeom JH, Lee K. RraA rescues Escherichia coli cells over-producing RNase E from growth arrest by modulating the ribonucleolytic activity. Biochem Biophys Res Commun. 2006 Jul 14;345(4):1372-6. Epub 2006 May 11. PMID:16725107 doi:10.1016/j.bbrc.2006.05.018
- ↑ Gao J, Lee K, Zhao M, Qiu J, Zhan X, Saxena A, Moore CJ, Cohen SN, Georgiou G. Differential modulation of E. coli mRNA abundance by inhibitory proteins that alter the composition of the degradosome. Mol Microbiol. 2006 Jul;61(2):394-406. Epub 2006 Jun 12. PMID:16771842 doi:10.1111/j.1365-2958.2006.05246.x
- ↑ Yeom JH, Go H, Shin E, Kim HL, Han SH, Moore CJ, Bae J, Lee K. Inhibitory effects of RraA and RraB on RNAse E-related enzymes imply conserved functions in the regulated enzymatic cleavage of RNA. FEMS Microbiol Lett. 2008 Aug;285(1):10-5. doi: 10.1111/j.1574-6968.2008.01205.x., Epub 2008 May 28. PMID:18510556 doi:10.1111/j.1574-6968.2008.01205.x
- ↑ Gorna MW, Pietras Z, Tsai YC, Callaghan AJ, Hernandez H, Robinson CV, Luisi BF. The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome. RNA. 2010 Jan 27. PMID:20106955 doi:rna.1858010
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