View source for 6ywp


==Structure of apo-CutA==
<StructureSection load='6ywp' size='340' side='right'caption='[[6ywp]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ywp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thett Thett]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YWP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YWP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THITE_2112714 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=578455 THETT])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ywp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ywp OCA], [http://pdbe.org/6ywp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ywp RCSB], [http://www.ebi.ac.uk/pdbsum/6ywp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ywp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Template-independent terminal ribonucleotide transferases (TENTs) catalyze the addition of nucleotide monophosphates to the 3'-end of RNA molecules regulating their fate. TENTs include poly(U) polymerases (PUPs) with a subgroup of 3' CUCU-tagging enzymes, such as CutA in Aspergillus nidulans. CutA preferentially incorporates cytosines, processively polymerizes only adenosines and does not incorporate or extend guanosines. The basis of this peculiar specificity remains to be established. Here, we describe crystal structures of the catalytic core of CutA in complex with an incoming non-hydrolyzable CTP analog and an RNA with three adenosines, along with biochemical characterization of the enzyme. The binding of GTP or a primer with terminal guanosine is predicted to induce clashes between 2-NH2 of the guanine and protein, which would explain why CutA is unable to use these ligands as substrates. Processive adenosine polymerization likely results from the preferential binding of a primer ending with at least two adenosines. Intriguingly, we found that the affinities of CutA for the CTP and UTP are very similar and the structures did not reveal any apparent elements for specific NTP binding. Thus, the properties of CutA likely result from an interplay between several factors, which may include a conformational dynamic process of NTP recognition.

Structure and mechanism of CutA, RNA nucleotidyl transferase with an unusual preference for cytosine.,Malik D, Kobylecki K, Krawczyk P, Poznanski J, Jakielaszek A, Napiorkowska A, Dziembowski A, Tomecki R, Nowotny M Nucleic Acids Res. 2020 Aug 12. pii: 5891578. doi: 10.1093/nar/gkaa647. PMID:32785623<ref>PMID:32785623</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ywp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thett]]
[[Category: Dziembowski, A]]
[[Category: Jakielaszek, A]]
[[Category: Kobylecki, K]]
[[Category: Krawczyk, P]]
[[Category: Malik, D]]
[[Category: Napiorkowska, A]]
[[Category: Nowotny, M]]
[[Category: Poznanski, J]]
[[Category: Tomecki, R]]
[[Category: Polymerase]]
[[Category: Rna binding protein]]
[[Category: Rna-binding protein]]
[[Category: Terminal nucleotide transferase]]