View source for 2rql


==Solution structure of the E. coli ribosome hibernation promoting factor HPF==
<StructureSection load='2rql' size='340' side='right'caption='[[2rql]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rql]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RQL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2rql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rql OCA], [https://pdbe.org/2rql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rql RCSB], [https://www.ebi.ac.uk/pdbsum/2rql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rql ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HPF_ECOLI HPF_ECOLI] During stationary phase, promotes and stabilizes dimerization of 70S ribosomes by the ribosome modulation factor (RMF), leading to the formation of inactive 100S ribosomes. May convert immature 90S particles formed by RMF into 100S ribosomes. May also function as a potential translational inhibitor.<ref>PMID:11168583</ref> <ref>PMID:16324148</ref> <ref>PMID:18174192</ref> <ref>PMID:19170772</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/rq/2rql_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=2rql ConSurf].
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== Publication Abstract from PubMed ==
The 70S Escherichia coli ribosome dimerizes to form an inactive 100S ribosome during stationary phase, which is called "ribosome hibernation". The hibernation promoting factor HPF plays a crucial role in 100S ribosome formation. However, YfiA, a known paralog of HPF inhibits 100S formation, although it shares high sequence similarity. Here, we report the first solution structure of HPF as determined by multi-dimensional NMR. HPF adopts betaalphabetabetabetaalpha-fold and the overall structure is similar to YfiA as expected. However, detailed structure comparison based on the determined structure in this study revealed that there are remarkable differences around the C-terminal portion of helix alpha2, which is not predicted by homology modeling. Furthermore, some acidic residues conserved only in HPF are located at the rim of the common basic patch.

Solution structure of the E. coli ribosome hibernation promoting factor HPF: Implications for the relationship between structure and function.,Sato A, Watanabe T, Maki Y, Ueta M, Yoshida H, Ito Y, Wada A, Mishima M Biochem Biophys Res Commun. 2009 Nov 27;389(4):580-5. Epub 2009 Sep 10. PMID:19747895<ref>PMID:19747895</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2rql" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Mishima M]]
[[Category: Sato A]]