5kal: Difference between revisions
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==Terminal uridylyl transferase 4 from Trypanosoma brucei with bound UTP and UpU== | ==Terminal uridylyl transferase 4 from Trypanosoma brucei with bound UTP and UpU== | ||
<StructureSection load='5kal' size='340' side='right' caption='[[5kal]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='5kal' size='340' side='right'caption='[[5kal]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kal]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KAL OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5kal]] is a 4 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=5KAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KAL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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]] 2.75Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5kal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kal OCA], [https://pdbe.org/5kal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kal RCSB], [https://www.ebi.ac.uk/pdbsum/5kal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kal ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TUT4_TRYB2 TUT4_TRYB2] Terminal uridylyltransferase which, specifically, catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs with a 3'-terminal U.<ref>PMID:17189640</ref> <ref>PMID:17785418</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5kal" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5kal" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[RNA uridylyltransferase|RNA uridylyltransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Trypanosoma brucei]] | ||
[[Category: | [[Category: Afasizhev R]] | ||
[[Category: | [[Category: Luecke H]] | ||
[[Category: | [[Category: Stagno JR]] | ||
Latest revision as of 12:57, 27 September 2023
Terminal uridylyl transferase 4 from Trypanosoma brucei with bound UTP and UpUTerminal uridylyl transferase 4 from Trypanosoma brucei with bound UTP and UpU
Structural highlights
FunctionTUT4_TRYB2 Terminal uridylyltransferase which, specifically, catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs with a 3'-terminal U.[1] [2] Publication Abstract from PubMedTerminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species. Uridylation plays a particularly prominent role in RNA processing pathways of kinetoplastid protists typified by the causative agent of African sleeping sickness, Trypanosoma brucei In mitochondria of this pathogen, most mRNAs are internally modified by U-insertion/deletion editing while guide RNAs and rRNAs are U-tailed. The founding member of TUTase family, RNA editing TUTase 1 (RET1), functions as a subunit of the 3' processome in uridylation of gRNA precursors and mature guide RNAs. Along with KPAP1 poly(A) polymerase, RET1 also participates in mRNA translational activation. RET1 is divergent from human TUTases and is essential for parasite viability in the mammalian host and the insect vector. Given its robust in vitro activity, RET1 represents an attractive target for trypanocide development. Here, we report high-resolution crystal structures of the RET1 catalytic core alone and in complex with UTP analogs. These structures reveal a tight docking of the conserved nucleotidyl transferase bi-domain module with a RET1-specific C2H2 zinc finger and RNA recognition (RRM) domains. Furthermore, we define RET1 region required for incorporation into the 3' processome, determinants for RNA binding, subunit oligomerization and processive UTP incorporation, and predict druggable pockets. RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting.,Rajappa-Titu L, Suematsu T, Munoz-Tello P, Long M, Demir O, Cheng KJ, Stagno JR, Luecke H, Amaro RE, Aphasizheva I, Aphasizhev R, Thore S Nucleic Acids Res. 2016 Oct 15. pii: gkw917. PMID:27744351[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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