4nl3: Difference between revisions
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==Crystal Structure of Listeria monocytogenes Hfq in complex with U6 RNA== | ==Crystal Structure of Listeria monocytogenes Hfq in complex with U6 RNA== | ||
<StructureSection load='4nl3' size='340' side='right' caption='[[4nl3]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='4nl3' size='340' side='right'caption='[[4nl3]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nl3]] is a 14 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4nl3]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NL3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</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=4nl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nl3 OCA], [https://pdbe.org/4nl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nl3 RCSB], [https://www.ebi.ac.uk/pdbsum/4nl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nl3 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/Q92C58_LISMO Q92C58_LISMO] 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4nl3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4nl3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Listeria monocytogenes]] | ||
[[Category: | [[Category: Brennan RG]] | ||
[[Category: | [[Category: Kovach AR]] | ||
Latest revision as of 19:58, 20 September 2023
Crystal Structure of Listeria monocytogenes Hfq in complex with U6 RNACrystal Structure of Listeria monocytogenes Hfq in complex with U6 RNA
Structural highlights
FunctionQ92C58_LISMO 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] Publication Abstract from PubMedHfq is a post-transcriptional regulator that binds U- and A-rich regions of sRNAs and their target mRNAs to stimulate their annealing in order to effect translation regulation and, often, to alter their stability. The functional importance of Hfq and its RNA-binding properties are relatively well understood in Gram-negative bacteria, whereas less is known about the RNA-binding properties of this riboregulator in Gram-positive species. Here, we describe the structure of Hfq from the Gram-positive pathogen Listeria monocytogenes in its RNA-free form and in complex with a U6 oligoribonucleotide. As expected, the protein takes the canonical hexameric toroidal shape of all other known Hfq structures. The U6 RNA binds on the "proximal face" in a pocket formed by conserved residues Q9, N42, F43, and K58. Additionally residues G5 and Q6 are involved in protein-nucleic and inter-subunit contacts that promote uracil specificity. Unlike Staphylococcus aureus (Sa) Hfq, Lm Hfq requires magnesium to bind U6 with high affinity. In contrast, the longer oligo-uridine, U16, binds Lm Hfq tightly in the presence or absence of magnesium, thereby suggesting the importance of additional residues on the proximal face and possibly the lateral rim in RNA interaction. Intrinsic tryptophan fluorescence quenching (TFQ) studies reveal, surprisingly, that Lm Hfq can bind (GU)3G and U6 on its proximal and distal faces, indicating a less stringent adenine-nucleotide specificity site on the distal face as compared to the Gram-positive Hfq proteins from Sa and Bacillus subtilis and suggesting as yet uncharacterized RNA-binding modes on both faces. Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes.,Kovach AR, Hoff KE, Canty JT, Orans J, Brennan RG RNA. 2014 Aug 22. PMID:25150227[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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