2y90: Difference between revisions

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-[[Image:2y90.png|left|200px]]
+==CRYSTAL STRUCTURE OF HFQ RIBOREGULATOR FROM E. COLI (P6 SPACE GROUP)==
+<StructureSection load='2y90' size='340' side='right' caption='[[2y90]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2y90]] is a 1 chain structure with 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=2Y90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y90 FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m7c|1m7c]], [[1oou|1oou]], [[1hk9|1hk9]], [[1oov|1oov]]</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=2y90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y90 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y90 RCSB], [http://www.ebi.ac.uk/pdbsum/2y90 PDBsum]</span></td></tr>
+</table>
+<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.
-{{STRUCTURE_2y90|  PDB=2y90  |  SCENE=  }}
+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>
-===CRYSTAL STRUCTURE OF HFQ RIBOREGULATOR FROM E. COLI (P6 SPACE GROUP)===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_12853626}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[2y90]] is a 1 chain structure with 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=2Y90 OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:012853626</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
 [[Category: Basquin, J.]]