6ywo

CutA in complex with A3 RNA

spinqualitylabelsall models 6ywo, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ywo is a 8 chain structure with sequence from Thermothielavioides terrestris NRRL 8126 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CL, MG, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G2R014_THETT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CutA1 3D structures

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