6l7v

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Current revision (10:45, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6l7v' size='340' side='right'caption='[[6l7v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6l7v' size='340' side='right'caption='[[6l7v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6l7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trycc Trycc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L7V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6l7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi_strain_CL_Brener Trypanosoma cruzi strain CL Brener]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L7V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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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]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tc00.1047053508479.390 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=353153 TRYCC])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=6l7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l7v OCA], [https://pdbe.org/6l7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l7v RCSB], [https://www.ebi.ac.uk/pdbsum/6l7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l7v ProSAT]</span></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=6l7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l7v OCA], [https://pdbe.org/6l7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l7v RCSB], [https://www.ebi.ac.uk/pdbsum/6l7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l7v ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q4E2I1_TRYCC Q4E2I1_TRYCC]
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RNA triphosphatase catalyzes the first step in mRNA cap formation, hydrolysis of the terminal phosphate from the nascent mRNA transcript. The RNA triphosphatase from the protozoan parasite Trypanosoma cruzi, TcCet1, belongs to the family of triphosphate tunnel metalloenzymes (TTMs). TcCet1 is a promising antiprotozoal drug target because the mechanism and structure of the protozoan RNA triphosphatases are completely different from those of the RNA triphosphatases found in mammalian and arthropod hosts. Here, we report several crystal structures of the catalytically active form of TcCet1 complexed with a divalent cation and an inorganic tripolyphosphate in the active-site tunnel at 2.20-2.51 A resolutions. The structures revealed that the overall structure, the architecture of the tunnel, and the arrangement of the metal-binding site in TcCet1 are similar to those in other TTM proteins. On the basis of the position of three sulfate ions that cocrystallized on the positively charged surface of the protein and results obtained from mutational analysis, we identified an RNA-binding site in TcCet1. We conclude that the 5'-end of the triphosphate RNA substrate enters the active-site tunnel directionally. The structural information reported here provides valuable insight into designing inhibitors that could specifically block the entry of the triphosphate RNA substrate into the TTM-type RNA triphosphatases of T. cruzi and related pathogens.
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Crystal structures of the RNA triphosphatase from Trypanosoma cruzi provide insights into how it recognizes the 5'-end of the RNA substrate.,Takagi Y, Kuwabara N, Dang TT, Furukawa K, Ho CK J Biol Chem. 2020 Jul 3;295(27):9076-9086. doi: 10.1074/jbc.RA119.011811. Epub, 2020 May 7. PMID:32381506<ref>PMID:32381506</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6l7v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Trycc]]
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[[Category: Trypanosoma cruzi strain CL Brener]]
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[[Category: Ho, K]]
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[[Category: Ho K]]
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[[Category: Kuwabara, N]]
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[[Category: Kuwabara N]]
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[[Category: Hydrolase]]
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[[Category: Mrna capping]]
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[[Category: Rna triphosphatase]]
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Current revision

Crystal structure of Cet1 from Trypanosoma cruzi in complex with tripolyphosphate, manganese and iodide ions.

PDB ID 6l7v

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