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==Structure of the C-terminal domain of the Escherichia Coli ProQ RNA binding protein==
<StructureSection load='5nbb' size='340' side='right'caption='[[5nbb]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nbb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NBB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5nbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbb OCA], [https://pdbe.org/5nbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nbb RCSB], [https://www.ebi.ac.uk/pdbsum/5nbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PROQ_ECOLI PROQ_ECOLI] RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism.[HAMAP-Rule:MF_00749]<ref>PMID:21381725</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The protein ProQ has recently been identified as a global small noncoding RNA-binding protein in Salmonella, and a similar role is anticipated for its numerous homologs in divergent bacterial species. We report the solution structure of Escherichia coli ProQ, revealing an N-terminal FinO-like domain, a C-terminal domain that unexpectedly has a Tudor domain fold commonly found in eukaryotes, and an elongated bridging intradomain linker that is flexible but nonetheless incompressible. Structure-based sequence analysis suggests that the Tudor domain was acquired through horizontal gene transfer and gene fusion to the ancestral FinO-like domain. Through a combination of biochemical and biophysical approaches, we have mapped putative RNA-binding surfaces on all three domains of ProQ and modeled the protein's conformation in the apo and RNA-bound forms. Taken together, these data suggest how the FinO, Tudor, and linker domains of ProQ cooperate to recognize complex RNA structures and serve to promote RNA-mediated regulation.

Structure of the Escherichia coli ProQ RNA-binding protein.,Gonzalez GM, Hardwick SW, Maslen SL, Skehel JM, Holmqvist E, Vogel J, Bateman A, Luisi BF, Broadhurst RW RNA. 2017 May;23(5):696-711. doi: 10.1261/rna.060343.116. Epub 2017 Feb 13. PMID:28193673<ref>PMID:28193673</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nbb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Bateman A]]
[[Category: Broadhurst R]]
[[Category: Gonzales G]]
[[Category: Hardwick S]]
[[Category: Holmqvist E]]
[[Category: Luisi B]]
[[Category: Maslen S]]
[[Category: Skehel M]]
[[Category: Vogel J]]