4pno: Difference between revisions

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-'''Unreleased structure'''
-The entry 4pno is ON HOLD
+==Escherichia coli Hfq-RNA complex at 0.97 A Resolution==
+<StructureSection load='4pno' size='340' side='right'caption='[[4pno]], [[Resolution|resolution]] 0.97&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pno]] is a 1 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=4PNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PNO FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.97&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></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=4pno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pno OCA], [https://pdbe.org/4pno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pno RCSB], [https://www.ebi.ac.uk/pdbsum/4pno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pno ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/C1IFD2_ECOLX C1IFD2_ECOLX] RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA-mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 A resolution, revealing the Hfq-RNA interaction in exceptional detail.
-Authors: Schulz, E.C., Barabas, O.
+Structure of an Escherichia coli Hfq:RNA complex at 0.97 A resolution.,Schulz EC, Barabas O Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1492-7. doi:, 10.1107/S2053230X14020044. Epub 2014 Oct 31. PMID:25372815<ref>PMID:25372815</ref>
-Description: Escherichia coli Hfq-RNA complex at 0.97 A Resolution
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4pno" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Protein Hfq 3D structures|Protein Hfq 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Barabas O]]
+[[Category: Schulz EC]]