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6e4n

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(New page: '''Unreleased structure''' The entry 6e4n is ON HOLD until Paper Publication Authors: Schumacher, M.A. Description: Structure of the T. brucei TbRGG2 RRM domain: apo R3 crystal form [[...)
Current revision (06:18, 11 October 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6e4n is ON HOLD until Paper Publication
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==Structure of the T. brucei TbRGG2 RRM domain: apo R3 crystal form==
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<StructureSection load='6e4n' size='340' side='right'caption='[[6e4n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6e4n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E4N FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.801&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e4n OCA], [https://pdbe.org/6e4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e4n RCSB], [https://www.ebi.ac.uk/pdbsum/6e4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e4n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q389P7_TRYB2 Q389P7_TRYB2]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Kinetoplastid RNA (kRNA) editing takes place in the mitochondria of kinetoplastid protists and creates translatable mRNAs by uridine insertion/deletion. Extensively edited (pan-edited) transcripts contain quadruplex forming guanine stretches, which must be remodeled to promote uridine insertion/deletion. Here we show that the RRM domain of the essential kRNA-editing factor TbRGG2 binds poly(G) and poly(U) RNA and can unfold both. A region C-terminal to the RRM mediates TbRGG2 dimerization, enhancing RNA binding. A RRM-U4 RNA structure reveals a unique RNA-binding mechanism in which the two RRMs of the dimer employ aromatic residues outside the canonical RRM RNA-binding motifs to encase and wrench open the RNA, while backbone atoms specify the uridine bases. Notably, poly(G) RNA is bound via a different binding surface. Thus, these data indicate that TbRGG2 RRM can bind and remodel several RNA substrates suggesting how it might play multiple roles in the kRNA editing process.
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Authors: Schumacher, M.A.
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The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA.,Travis B, Shaw PLR, Liu B, Ravindra K, Iliff H, Al-Hashimi HM, Schumacher MA Nucleic Acids Res. 2018 Dec 14. pii: 5245446. doi: 10.1093/nar/gky1259. PMID:30544166<ref>PMID:30544166</ref>
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Description: Structure of the T. brucei TbRGG2 RRM domain: apo R3 crystal form
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Schumacher, M.A]]
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<div class="pdbe-citations 6e4n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Trypanosoma brucei]]
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[[Category: Schumacher MA]]

Current revision

Structure of the T. brucei TbRGG2 RRM domain: apo R3 crystal form

PDB ID 6e4n

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