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| ==Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase== | | ==Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase== |
| <StructureSection load='4e8f' size='340' side='right' caption='[[4e8f]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4e8f' size='340' side='right'caption='[[4e8f]], [[Resolution|resolution]] 2.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4e8f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E8F FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4e8f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E8F FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.6Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e7x|4e7x]], [[4e80|4e80]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cid1, SPAC19D5.03 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=4e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e8f OCA], [https://pdbe.org/4e8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e8f RCSB], [https://www.ebi.ac.uk/pdbsum/4e8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e8f ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e8f OCA], [http://pdbe.org/4e8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e8f RCSB], [http://www.ebi.ac.uk/pdbsum/4e8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e8f ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CID1_SCHPO CID1_SCHPO]] Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis. | | [https://www.uniprot.org/uniprot/CID1_SCHPO CID1_SCHPO] Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Cytoplasmic terminal uridylyl transferases comprise a conserved family of enzymes that negatively regulate the stability or biological activity of a variety of eukaryotic RNAs, including mRNAs and tumor-suppressor let-7 microRNAs. Here we describe crystal structures of the Schizosaccharomyces pombe cytoplasmic terminal uridylyl transferase Cid1 in two apo conformers and bound to UTP. We demonstrate that a single histidine residue, conserved in mammalian Cid1 orthologs, is responsible for discrimination between UTP and ATP. We also describe a new high-affinity RNA substrate-binding mechanism of Cid1, which is essential for enzymatic activity and is mediated by three basic patches across the surface of the enzyme. Overall, our structures provide a basis for understanding the activity of Cid1 and a mechanism of UTP selectivity conserved in its human orthologs, suggesting potential implications for anticancer drug design.
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| Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase.,Yates LA, Fleurdepine S, Rissland OS, De Colibus L, Harlos K, Norbury CJ, Gilbert RJ Nat Struct Mol Biol. 2012 Jul 1. doi: 10.1038/nsmb.2329. PMID:22751018<ref>PMID:22751018</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4e8f" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Poly(A) RNA polymerase protein Cid1|Poly(A) RNA polymerase protein Cid1]] | | *[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]] |
| *[[RNA polymerase|RNA polymerase]]
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Fission yeast]] | | [[Category: Large Structures]] |
| [[Category: DeColibus, L]] | | [[Category: Schizosaccharomyces pombe 972h-]] |
| [[Category: Fleurdepine, S]] | | [[Category: DeColibus L]] |
| [[Category: Gilbert, R J.C]] | | [[Category: Fleurdepine S]] |
| [[Category: Harlos, K]] | | [[Category: Gilbert RJC]] |
| [[Category: Norbury, C J]] | | [[Category: Harlos K]] |
| [[Category: Rissland, O S]] | | [[Category: Norbury CJ]] |
| [[Category: Yates, L A]] | | [[Category: Rissland OS]] |
| [[Category: Beta polymerase-like nucleotidyl transferase]]
| | [[Category: Yates LA]] |
| [[Category: Cytoplasmic]]
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| [[Category: Rna]]
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| [[Category: Terminal uridine transferase]]
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| [[Category: Transferase]]
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| [[Category: Utp]]
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