4wc2 | pdb_00004wc2

Crystal structure of tRNA nucleotidyltransferase complexed with a primer tRNA and an incoming ATP analog

spinqualitylabelsall models 4wc2, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wc2 is a 2 chain structure with sequence from Aquifex aeolicus VF5 and Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: APC, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AATNT_AQUAE tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA (PubMed:11701927, PubMed:25914059). Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency (PubMed:25914059). Publication Abstract from PubMed The 3'-terminal CCA (C74C75A76-3') of tRNA is required for protein synthesis. In Aquifex aeolicus, the CCA-3' is synthesized by CC-adding and A-adding enzymes, although in most organisms, CCA is synthesized by a single CCA-adding enzyme. The mechanisms by which the A-adding enzyme adds only A76, but not C74C75, onto tRNA remained elusive. The complex structures of the enzyme with various tRNAs revealed the presence of a single tRNA binding site on the enzyme, with the enzyme measuring the acceptor-TPsiC helix length of tRNA. The 3'-C75 of tRNA lacking A76 can reach the active site and the size and shape of the nucleotide binding pocket at the insertion stage are suitable for ATP. The 3'-C74 of tRNA lacking C75A76 cannot reach the active site, although CTP or ATP can bind the active pocket. Thus, the A-adding enzyme adds only A76, but not C74C75, onto tRNA. Measurement of Acceptor-TPsiC Helix Length of tRNA for Terminal A76-Addition by A-Adding Enzyme.,Yamashita S, Martinez A, Tomita K Structure. 2015 May 5;23(5):830-42. doi: 10.1016/j.str.2015.03.013. Epub 2015 Apr, 23. PMID:25914059 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Poly(A) Polymerase

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