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4e80

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Current revision (11:02, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e80]] is a 4 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=4E80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E80 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e80]] is a 4 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=4E80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E80 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=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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]] 3.02&#8491;</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=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=4e80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e80 OCA], [https://pdbe.org/4e80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e80 RCSB], [https://www.ebi.ac.uk/pdbsum/4e80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e80 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=4e80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e80 OCA], [https://pdbe.org/4e80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e80 RCSB], [https://www.ebi.ac.uk/pdbsum/4e80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e80 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<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&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 4e80" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]]
*[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase

PDB ID 4e80

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