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| | <StructureSection load='2v9k' size='340' side='right'caption='[[2v9k]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2v9k' size='340' side='right'caption='[[2v9k]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v9k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2V9K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v9k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V9K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2v9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9k OCA], [http://pdbe.org/2v9k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v9k RCSB], [http://www.ebi.ac.uk/pdbsum/2v9k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9k ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2v9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9k OCA], [https://pdbe.org/2v9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v9k RCSB], [https://www.ebi.ac.uk/pdbsum/2v9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PUS10_HUMAN PUS10_HUMAN]] Pseudouridylate synthases catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. PUS10 catalyzes the formation of the universal psi55 in the GC loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell death via activation of procaspase 8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death.<ref>PMID:14527409</ref> <ref>PMID:19712588</ref> | + | [https://www.uniprot.org/uniprot/PUS10_HUMAN PUS10_HUMAN] Pseudouridylate synthases catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. PUS10 catalyzes the formation of the universal psi55 in the GC loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell death via activation of procaspase 8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death.<ref>PMID:14527409</ref> <ref>PMID:19712588</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hornsby, M]] | + | [[Category: Hornsby M]] |
| - | [[Category: Kreusch, A]] | + | [[Category: Kreusch A]] |
| - | [[Category: McCleverty, C J]] | + | [[Category: McCleverty CJ]] |
| - | [[Category: Spraggon, G]] | + | [[Category: Spraggon G]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pseudouridine synthase]]
| + | |
| - | [[Category: Pus10]]
| + | |
| - | [[Category: Rna modification]]
| + | |
| - | [[Category: Thump domain]]
| + | |
| Structural highlights
Function
PUS10_HUMAN Pseudouridylate synthases catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. PUS10 catalyzes the formation of the universal psi55 in the GC loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell death via activation of procaspase 8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Pseudouridine (Psi) synthases catalyze the formation of one or more specific Psis in structured RNAs. Five families of Psi synthases have been characterized based on sequence homology. Pus10 has no significant sequence homology to these defined families and therefore represents a new family of Psi synthases. Initial characterization studies show that an archael Pus10 catalyzes the universally conserved Psi55 in tRNA. We present here the crystal structure of human Pus10 at 2.0 A resolution, which is the first structural description from this novel Psi synthase family. Pus10 is a crescent-shaped molecule with two domains, the universally conserved Psi synthase catalytic domain and a THUMP-containing domain, which is unique to the Pus10 family. Superposition of the catalytic domains of Pus10 and other Psi synthases identifies the full set of conserved Psi synthase active site residues indicating that Pus10 likely employs a similar catalytic mechanism to other Psi synthases. The Pus10 active site is located in a deep pocket of a basic cleft adjacent to flexible thumb and forefinger loops, which could provide further stabilization for binding the RNA substrate. Modeling studies demonstrate that the cleft between the catalytic and accessory domain is large enough and electrostatically compatible to accommodate an RNA stem and support the role of the N-terminal domain as an accessory RNA-binding domain.
Crystal structure of human Pus10, a novel pseudouridine synthase.,McCleverty CJ, Hornsby M, Spraggon G, Kreusch A J Mol Biol. 2007 Nov 9;373(5):1243-54. Epub 2007 Aug 29. PMID:17900615[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aza-Blanc P, Cooper CL, Wagner K, Batalov S, Deveraux QL, Cooke MP. Identification of modulators of TRAIL-induced apoptosis via RNAi-based phenotypic screening. Mol Cell. 2003 Sep;12(3):627-37. PMID:14527409
- ↑ Park SY, Shin JN, Woo HN, Piya S, Moon AR, Seo YW, Seol DW, Kim TH. DOBI is cleaved by caspases during TRAIL-induced apoptotic cell death. BMB Rep. 2009 Aug 31;42(8):511-5. PMID:19712588
- ↑ McCleverty CJ, Hornsby M, Spraggon G, Kreusch A. Crystal structure of human Pus10, a novel pseudouridine synthase. J Mol Biol. 2007 Nov 9;373(5):1243-54. Epub 2007 Aug 29. PMID:17900615 doi:10.1016/j.jmb.2007.08.053
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