4e8f: Difference between revisions

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 == Structural highlights ==
 <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" id="ligandDat"><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]] 2.6&#8491;</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='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>
 </table>
 == Function ==
-[[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.
+[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;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4e8f" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>