4v2s: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v2s]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V2S FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v2s]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V2S 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=4v2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v2s RCSB], [http://www.ebi.ac.uk/pdbsum/4v2s PDBsum]</span></td></tr> | </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=4v2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2s OCA], [http://pdbe.org/4v2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v2s RCSB], [http://www.ebi.ac.uk/pdbsum/4v2s PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4v2s" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:03, 16 December 2015
Crystal structure of Hfq in complex with the sRNA RydCCrystal structure of Hfq in complex with the sRNA RydC
Structural highlights
Function[HFQ_ECOLI] 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. Involved in the regulation of stress responses mediated by the sigma factors RpoS, sigma-E and sigma-32. Binds with high specificity to tRNAs. In vitro, stimulates synthesis of long tails by poly(A) polymerase I. Required for RNA phage Qbeta replication.[1] [2] [3] [4] [5] Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.[6] [7] [8] [9] [10] Publication Abstract from PubMedBacterial small RNAs (sRNAs) are key elements of regulatory networks that modulate gene expression. The sRNA RydC of Salmonella sp. and Escherichia coli is an example of this class of riboregulators. Like many other sRNAs, RydC bears a 'seed' region that recognises specific transcripts through base-pairing, and its activities are facilitated by the RNA chaperone Hfq. The crystal structure of RydC in complex with E. coli Hfq at 3.48 A resolution illuminates how the protein interacts with and presents the sRNA for target recognition. Consolidating the protein-RNA complex is a host of distributed interactions mediated by the natively unstructured termini of Hfq. Based on the structure and other data, we propose a model for a dynamic effector complex comprising Hfq, small RNA, and the cognate mRNA target. Recognition of the small regulatory RNA RydC by the bacterial Hfq protein.,Dimastrogiovanni D, Frohlich KS, Bandyra KJ, Bruce HA, Hohensee S, Vogel J, Luisi BF Elife. 2014 Dec 31;3. doi: 10.7554/eLife.05375. PMID:25551292[11] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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