1q5x

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[[Image:1q5x.jpg|left|200px]]
 
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{{Structure
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==Structure of OF RRAA (MENG), a protein inhibitor of RNA processing==
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|PDB= 1q5x |SIZE=350|CAPTION= <scene name='initialview01'>1q5x</scene>, resolution 2.0&Aring;
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<StructureSection load='1q5x' size='340' side='right'caption='[[1q5x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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&#8491;</td></tr>
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|GENE= MENG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=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>
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}}
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</table>
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== Function ==
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'''Structure of OF RRAA (MENG), a protein inhibitor of RNA processing'''
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q5/1q5x_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1Q5X is a [[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].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</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].
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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://www.ncbi.nlm.nih.gov/pubmed/14499605 14499605]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gao, J.]]
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[[Category: Gao J]]
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[[Category: Georgiou, G.]]
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[[Category: Georgiou G]]
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[[Category: Monzingo, A F.]]
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[[Category: Monzingo AF]]
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[[Category: Qiu, J.]]
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[[Category: Qiu J]]
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[[Category: Robertus, J D.]]
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[[Category: Robertus JD]]
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[[Category: 3-layer sandwich]]
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[[Category: alpha-beta structure]]
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[[Category: antiparallel beta sheet]]
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[[Category: parallel beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:33:24 2008''
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Current revision

Structure of OF RRAA (MENG), a protein inhibitor of RNA processing

PDB ID 1q5x

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