3eaq: Difference between revisions

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OCA

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 ==Novel dimerization motif in the DEAD box RNA helicase Hera form 2, complete dimer, symmetric==
-<StructureSection load='3eaq' size='340' side='right' caption='[[3eaq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3eaq' size='340' side='right'caption='[[3eaq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3eaq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3eaq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ear|3ear]], [[3eas|3eas]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1895 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=3eaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eaq OCA], [https://pdbe.org/3eaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eaq RCSB], [https://www.ebi.ac.uk/pdbsum/3eaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eaq ProSAT]</span></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=3eaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eaq OCA], [http://pdbe.org/3eaq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eaq RCSB], [http://www.ebi.ac.uk/pdbsum/3eaq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eaq ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q72GF3_THET2 Q72GF3_THET2]
 == 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/ea/3eaq_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3eaq_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 19: / Line 20: @@
 </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=3eaq ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-DEAD box helicases are involved in nearly all aspects of RNA metabolism. They share a common helicase core, and may comprise additional domains that contribute to RNA binding. The Thermus thermophilus helicase Hera is the first dimeric DEAD box helicase. Crystal structures of Hera fragments reveal a bipartite C-terminal domain with a novel dimerization motif and an RNA-binding module. We provide a first glimpse on the additional RNA-binding module outside the Hera helicase core. The dimerization and RNA-binding domains are connected to the C-terminal RecA domain by a hinge region that confers exceptional flexibility onto the helicase, allowing for different juxtapositions of the RecA-domains in the dimer. Combination of the previously determined N-terminal Hera structure with the C-terminal Hera structures allows generation of a model for the entire Hera dimer, where two helicase cores can work in conjunction on large RNA substrates.
-A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.,Klostermeier D, Rudolph MG Nucleic Acids Res. 2009 Feb;37(2):421-30. Epub 2008 Dec 2. PMID:19050012<ref>PMID:19050012</ref>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+*[[Helicase 3D structures|Helicase 3D structures]]
-</div>
-<div class="pdbe-citations 3eaq" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Thet2]]
+[[Category: Large Structures]]
-[[Category: Klostermeier, D]]
+[[Category: Thermus thermophilus HB27]]
-[[Category: Rudolph, M G]]
+[[Category: Klostermeier D]]
-[[Category: Atp-binding]]
+[[Category: Rudolph MG]]
-[[Category: Dead box rna helicase]]
-[[Category: Dimer]]
-[[Category: Helicase]]
-[[Category: Hydrolase]]
-[[Category: Nucleotide-binding]]