1q5x
From Proteopedia
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==Structure of OF RRAA (MENG), a protein inhibitor of RNA processing== | ==Structure of OF RRAA (MENG), a protein inhibitor of RNA processing== | ||
| - | <StructureSection load='1q5x' size='340' side='right' caption='[[1q5x]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1q5x' size='340' side='right'caption='[[1q5x]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1q5x]] is a 3 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </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'>[ | + | <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> |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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:14499605<ref>PMID:14499605</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1q5x" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: Gao | + | [[Category: Large Structures]] |
| - | [[Category: Georgiou | + | [[Category: Gao J]] |
| - | [[Category: Monzingo | + | [[Category: Georgiou G]] |
| - | [[Category: Qiu | + | [[Category: Monzingo AF]] |
| - | [[Category: Robertus | + | [[Category: Qiu J]] |
| - | + | [[Category: Robertus JD]] | |
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Current revision
Structure of OF RRAA (MENG), a protein inhibitor of RNA processing
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