2yht: Difference between revisions

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 <StructureSection load='2yht' size='340' side='right'caption='[[2yht]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yht]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YHT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yht]] is a 12 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=2YHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YHT FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m7c|1m7c]], [[2y90|2y90]], [[1oou|1oou]], [[1hk9|1hk9]], [[1oov|1oov]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=2yht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yht OCA], [https://pdbe.org/2yht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yht RCSB], [https://www.ebi.ac.uk/pdbsum/2yht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yht ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HFQ_ECOLI 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.<ref>PMID:805130</ref> <ref>PMID:10677490</ref> <ref>PMID:11222598</ref> <ref>PMID:17158661</ref> <ref>PMID:19909729</ref>   Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.<ref>PMID:805130</ref> <ref>PMID:10677490</ref> <ref>PMID:11222598</ref> <ref>PMID:17158661</ref> <ref>PMID:19909729</ref>
+[https://www.uniprot.org/uniprot/HFQ_ECOLI 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.<ref>PMID:805130</ref> <ref>PMID:10677490</ref> <ref>PMID:11222598</ref> <ref>PMID:17158661</ref> <ref>PMID:19909729</ref>   Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.<ref>PMID:805130</ref> <ref>PMID:10677490</ref> <ref>PMID:11222598</ref> <ref>PMID:17158661</ref> <ref>PMID:19909729</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qbeta phage RNA replication. During the last decade, it was shown to be involved in many RNA processing events and remote sequence homology indicated a link to spliceosomal Sm proteins. We report the crystal structure of the E.coli Hfq protein showing that its monomer displays a characteristic Sm-fold and forms a homo-hexamer, in agreement with former biochemical data. Overall, the structure of the E.coli Hfq ring is similar to the one recently described for Staphylococcus aureus. This confirms that bacteria contain a hexameric Sm-like protein which is likely to be an ancient and less specialized form characterized by a relaxed RNA binding specificity. In addition, we identified an Hfq ortholog in the archaeon Methanococcus jannaschii which lacks a classical Sm/Lsm gene. Finally, a detailed structural comparison shows that the Sm-fold is remarkably well conserved in bacteria, Archaea and Eukarya, and represents a universal and modular building unit for oligomeric RNA binding proteins.
-Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli.,Sauter C, Basquin J, Suck D Nucleic Acids Res. 2003 Jul 15;31(14):4091-8. PMID:12853626<ref>PMID:12853626</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2yht" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Basquin, J]]
+[[Category: Basquin J]]
-[[Category: Sauter, C]]
+[[Category: Sauter C]]
-[[Category: Chaperone]]
-[[Category: Rna chaperone]]