6ywo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==CutA in complex with A3 RNA== | ||
<StructureSection load='6ywo' size='340' side='right'caption='[[6ywo]]' scene=''> | <StructureSection load='6ywo' size='340' side='right'caption='[[6ywo]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ywo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothielavioides_terrestris_NRRL_8126 Thermothielavioides terrestris NRRL 8126] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YWO FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6ywo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ywo OCA], [https://pdbe.org/6ywo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ywo RCSB], [https://www.ebi.ac.uk/pdbsum/6ywo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ywo ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G2R014_THETT G2R014_THETT] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ywo" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CutA1 3D structures|CutA1 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: Thermothielavioides terrestris NRRL 8126]] | |||
[[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]] | |||
Latest revision as of 16:21, 6 November 2024
CutA in complex with A3 RNACutA in complex with A3 RNA
Structural highlights
FunctionPublication Abstract from PubMedTemplate-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||