View source for 4nkt


==Structure of Cid1 in complex with the UTP analog UMPNPP==
<StructureSection load='4nkt' size='340' side='right'caption='[[4nkt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nkt]] 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=4NKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NKT 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2KH:5-O-[(S)-HYDROXY{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]AMINO}PHOSPHORYL]URIDINE'>2KH</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4nkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nkt OCA], [https://pdbe.org/4nkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nkt RCSB], [https://www.ebi.ac.uk/pdbsum/4nkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nkt 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 ==
The addition of uridine nucleotide by the poly(U) polymerase (PUP) enzymes has a demonstrated impact on various classes of RNAs such as microRNAs (miRNAs), histone-encoding RNAs and messenger RNAs. Cid1 protein is a member of the PUP family. We solved the crystal structure of Cid1 in complex with non-hydrolyzable UMPNPP and a short dinucleotide compound ApU. These structures revealed new residues involved in substrate/product stabilization. In particular, one of the three catalytic aspartate residues explains the RNA dependence of its PUP activity. Moreover, other residues such as residue N165 or the beta-trapdoor are shown to be critical for Cid1 activity. We finally suggest that the length and sequence of Cid1 substrate RNA influence the balance between Cid1's processive and distributive activities. We propose that particular processes regulated by PUPs require the enzymes to switch between the two types of activity as shown for the miRNA biogenesis where PUPs can either promote DICER cleavage via short U-tail or trigger miRNA degradation by adding longer poly(U) tail. The enzymatic properties of these enzymes may be critical for determining their particular function in vivo.

A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.,Munoz-Tello P, Gabus C, Thore S Nucleic Acids Res. 2013 Dec 9. PMID:24322298<ref>PMID:24322298</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nkt" 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: Gabus C]]
[[Category: Munoz-Tello P]]
[[Category: Thore S]]