View source for 4ud5


==Structural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl Transferase Activity==
<StructureSection load='4ud5' size='340' side='right'caption='[[4ud5]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ud5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UD5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52&#8491;</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=4ud5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud5 OCA], [https://pdbe.org/4ud5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ud5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ud5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ud5 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Terminal uridylyl transferases (TUTs) are responsible for the post-transcriptional addition of uridyl residues to RNA 3' ends, leading in some cases to altered stability. The Schizosaccharomyces pombe TUT Cid1 is a model enzyme that has been characterized structurally at moderate resolution and provides insights into the larger and more complex mammalian TUTs, ZCCHC6 and ZCCHC11. Here, we report a higher resolution (1.74 A) crystal structure of Cid1 that provides detailed evidence for uracil selection via the dynamic flipping of a single histidine residue. We also describe a novel closed conformation of the enzyme that may represent an intermediate stage in a proposed product ejection mechanism. The structural insights gained, combined with normal mode analysis and biochemical studies, demonstrate that the plasticity of Cid1, particularly about a hinge region (N164-N165), is essential for catalytic activity, and provide an explanation for its distributive uridylyl transferase activity. We propose a model clarifying observed differences between the in vitro apparently processive activity and in vivo distributive monouridylylation activity of Cid1. We suggest that modulating the flexibility of such enzymes-for example by the binding of protein co-factors-may allow them alternatively to add single or multiple uridyl residues to the 3' termini of RNA molecules.

Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity.,Yates LA, Durrant BP, Fleurdepine S, Harlos K, Norbury CJ, Gilbert RJ Nucleic Acids Res. 2015 Mar 11;43(5):2968-79. doi: 10.1093/nar/gkv122. Epub 2015 , Feb 20. PMID:25712096<ref>PMID:25712096</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ud5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Durrant BP]]
[[Category: Fleurdepine S]]
[[Category: Gilbert RJC]]
[[Category: Harlos K]]
[[Category: Norbury CJ]]
[[Category: Yates LA]]