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| | <StructureSection load='5x15' size='340' side='right'caption='[[5x15]], [[Resolution|resolution]] 3.09Å' scene=''> | | <StructureSection load='5x15' size='340' side='right'caption='[[5x15]], [[Resolution|resolution]] 3.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x15]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X15 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X15 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x15]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X15 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCO7163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.094Å</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=5x15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x15 OCA], [http://pdbe.org/5x15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x15 RCSB], [http://www.ebi.ac.uk/pdbsum/5x15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x15 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=5x15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x15 OCA], [https://pdbe.org/5x15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x15 RCSB], [https://www.ebi.ac.uk/pdbsum/5x15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x15 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q9FBS9_STRCO Q9FBS9_STRCO] |
| - | Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-terminal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, exhibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long alpha-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Truncation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our findings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension alpha-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.
| + | |
| - | | + | |
| - | Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family.,Park N, Heo J, Song S, Jo I, Lee K, Ha NC J Microbiol. 2017 May;55(5):388-395. doi: 10.1007/s12275-017-7053-8. Epub 2017, Apr 29. PMID:28455590<ref>PMID:28455590</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5x15" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strco]]
| + | [[Category: Ha N-C]] |
| - | [[Category: Ha, N C]] | + | [[Category: Jo I]] |
| - | [[Category: Jo, I]] | + | [[Category: Park N]] |
| - | [[Category: Park, N]] | + | |
| - | [[Category: Rnase es inhibitor]]
| + | |
| - | [[Category: Rraa protein family]]
| + | |
| - | [[Category: Rraas2]]
| + | |
| - | [[Category: Streptomyces coelicolor]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase inhibitor]]
| + | |
