6s10

<table><tr><td colspan='2'>[[6s10]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S10 FirstGlance]. <br>

</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=6s10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s10 OCA], [https://pdbe.org/6s10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s10 RCSB], [https://www.ebi.ac.uk/pdbsum/6s10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s10 ProSAT]</span></td></tr>

== Function ==

[https://www.uniprot.org/uniprot/Q5ZUU4_LEGPH Q5ZUU4_LEGPH]

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== Publication Abstract from PubMed ==

Small regulatory RNAs (sRNAs) play an important role for posttranscriptional gene regulation in bacteria. sRNAs recognize their target messenger RNAs (mRNAs) by base pairing, which is often facilitated by interactions with the bacterial RNA-binding proteins Hfq or ProQ. The FinO/ProQ RNA-binding protein domain was first discovered in the bacterial repressor of conjugation, FinO. Since then, the functional role of FinO/ProQ-like proteins in posttranscriptional gene regulation was extensively studied in particular in the enterobacteria E. coli and Salmonella enterica and a wide range of sRNA-targets was identified for these proteins. In addition, enterobacterial ProQ homologs also recognize and protect the 3'-ends of a number of mRNAs from exonucleolytic degradation. However, the RNA-binding properties of FinO/ProQ proteins with regard to the recognition of different RNA targets are not yet fully understood. Here, we present the solution NMR structure of the so far functionally uncharacterized ProQ homolog Lpp1663 from Legionella pneumophila as a newly confirmed member and a minimal model system of the FinO/ProQ protein family. In addition, we characterize the RNA-binding preferences of Lpp1663 with high resolution NMR spectroscopy and isothermal titration calorimetry (ITC). Our results suggest a binding preference for single-stranded uridine-rich RNAs in the vicinity of stable stem-loop structures. According to chemical shift perturbation experiments, the single-stranded U-rich RNAs interact mainly with a conserved RNA-binding surface on the concave site of Lpp1663.

Solution structure and RNA-binding of a minimal ProQ-homolog from Legionella pneumophila (Lpp1663).,Immer C, Hacker C, Wohnert J RNA. 2020 Sep 28. pii: rna.077354.120. doi: 10.1261/rna.077354.120. PMID:32989045<ref>PMID:32989045</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 6s10" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Legionella pneumophila]]