1hk9: Difference between revisions

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-[[Image:1hk9.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1hk9", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1hk9|  PDB=1hk9  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI'''
+==Crystal structure of the Hfq protein from Escherichia coli==
+<StructureSection load='1hk9' size='340' side='right'caption='[[1hk9]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hk9]] is a 6 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=1HK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HK9 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]] 2.15&#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=1hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hk9 OCA], [https://pdbe.org/1hk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hk9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hk9 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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hk/1hk9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hk9 ConSurf].
+<div style="clear:both"></div>
+<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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-HK9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HK9 OCA].
+</div>
+<div class="pdbe-citations 1hk9" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/12853626 12853626]
+*[[Protein Hfq 3D structures|Protein Hfq 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Basquin, J.]]
+[[Category: Basquin J]]
-[[Category: Sauter, C.]]
+[[Category: Sauter C]]
-[[Category: Suck, D.]]
+[[Category: Suck D]]
-[[Category: Hfq]]
-[[Category: Pleiotropic regulator]]
-[[Category: Rna binding protein]]
-[[Category: Rna chaperone]]
-[[Category: Sm-like]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:56:13 2008''