5x15: Difference between revisions
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==Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase ES inhibitor RraA protein family== | |||
<StructureSection load='5x15' size='340' side='right' caption='[[5x15]], [[Resolution|resolution]] 3.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5x15]] is a 3 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X15 FirstGlance]. <br> | |||
</td></tr><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=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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Ha, N | <div class="pdbe-citations 5x15" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[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]] | |||
Revision as of 15:42, 17 May 2017
Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase ES inhibitor RraA protein family
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