2b51
From Proteopedia
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==Structural Basis for UTP Specificity of RNA Editing TUTases from Trypanosoma Brucei== | ==Structural Basis for UTP Specificity of RNA Editing TUTases from Trypanosoma Brucei== | ||
- | <StructureSection load='2b51' size='340' side='right' caption='[[2b51]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='2b51' size='340' side='right'caption='[[2b51]], [[Resolution|resolution]] 2.05Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2b51]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2b51]] 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=2B51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B51 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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=2b51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b51 OCA], [https://pdbe.org/2b51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b51 RCSB], [https://www.ebi.ac.uk/pdbsum/2b51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b51 ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/TUT2_TRYBB TUT2_TRYBB] Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core complex (RECC), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:12820966, PubMed:19465686, PubMed:20362585). Specifically, catalyzes the addition of one U to single-stranded RNA with a preference for a 3'-terminal A or G and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates (PubMed:12820966, PubMed:19465686, PubMed:20362585, PubMed:16281058). Essential for the survival of the bloodstream form (PubMed:16281058).<ref>PMID:12820966</ref> <ref>PMID:16281058</ref> <ref>PMID:19465686</ref> <ref>PMID:20362585</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2b51 ConSurf]. | </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=2b51 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Trypanosomatids are pathogenic protozoa that undergo a unique form of post-transcriptional RNA editing that inserts or deletes uridine nucleotides in many mitochondrial pre-mRNAs. Editing is catalyzed by a large multiprotein complex, the editosome. A key editosome enzyme, RNA editing terminal uridylyl transferase 2 (TUTase 2; RET2) catalyzes the uridylate addition reaction. Here, we report the 1.8 A crystal structure of the Trypanosoma brucei RET2 apoenzyme and its complexes with uridine nucleotides. This structure reveals that the specificity of the TUTase for UTP is determined by a crucial water molecule that is exquisitely positioned by the conserved carboxylates D421 and E424 to sense a hydrogen atom on the N3 position of the uridine base. The three-domain structure also unveils a unique domain arrangement not seen before in the nucleotidyltansferase superfamily, with a large domain insertion between the catalytic aspartates. This insertion is present in all trypanosomatid TUTases. We also show that TbRET2 is essential for survival of the bloodstream form of the parasite and therefore is a potential target for drug therapy. | ||
- | + | ==See Also== | |
- | + | *[[RNA uridylyltransferase|RNA uridylyltransferase]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
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[[Category: Trypanosoma brucei]] | [[Category: Trypanosoma brucei]] | ||
+ | [[Category: Deng J]] | ||
+ | [[Category: Ernst NL]] | ||
+ | [[Category: Hol WG]] | ||
+ | [[Category: Stuart KD]] | ||
+ | [[Category: Turley S]] |
Current revision
Structural Basis for UTP Specificity of RNA Editing TUTases from Trypanosoma Brucei
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