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1r3e
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1r3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r3e, resolution 2.1Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1r3e.gif|left|200px]]<br /><applet load="1r3e" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1r3e, resolution 2.1Å" /> | ||
| - | '''Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit'''<br /> | ||
| - | == | + | ==Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit== |
| - | + | <StructureSection load='1r3e' size='340' side='right'caption='[[1r3e]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1r3e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R3E 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FHU:(5S,6R)-5-FLUORO-6-HYDROXY-PSEUDOURIDINE-5-MONOPHOSPHATE'>FHU</scene></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=1r3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r3e OCA], [https://pdbe.org/1r3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r3e RCSB], [https://www.ebi.ac.uk/pdbsum/1r3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r3e ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRUB_THEMA TRUB_THEMA] Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (By similarity). | ||
| + | == 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/r3/1r3e_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=1r3e ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Guide-independent Pseudouridine synthase|Guide-independent Pseudouridine synthase]] | |
| - | + | *[[Pseudouridine synthase 3D structures|Pseudouridine synthase 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | [ | + | [[Category: Large Structures]] |
| - | [[Category: | + | |
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Agarwalla | + | [[Category: Agarwalla S]] |
| - | [[Category: Finer-Moore | + | [[Category: Finer-Moore J]] |
| - | [[Category: Moustakas | + | [[Category: Moustakas DT]] |
| - | [[Category: Pan | + | [[Category: Pan H]] |
| - | [[Category: Stroud | + | [[Category: Stroud RM]] |
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Current revision
Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit
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