9KMA
Crystal structure of the CCA-adding enzyme from Arabidopsis thaliana
Summary for 9KMA
| Entry DOI | 10.2210/pdb9kma/pdb |
| Descriptor | Polynucleotide adenylyltransferase family protein (1 entity in total) |
| Functional Keywords | cca-adding enzyme, trna processing, protein sorting, rna binding protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 66100.99 |
| Authors | |
| Primary citation | Wang, X.,Li, Y.Y.,Dou, Z.Y.,Wang, J.,Liu, L. Crystal structure of the CCA-adding enzyme from Arabidopsis thaliana . J Struct Biol X, 11:100127-100127, 2025 Cited by PubMed Abstract: The 3'-terminal CCA-end of tRNA is essential for the attachment of amino acids and correct positioning of the aminoacyl-tRNA in the ribosome. In higher plants, the CCA sequence is synthesized, maintained, and repaired by class-II CCA-adding enzymes encoded by a single nuclear gene but multi-targeted to the nucleus, cytoplasm, plastids, and mitochondria. The structure of plant class-II CCA-adding enzyme remains unsolved. Here we describe the crystal structure of CCA-adding enzyme from (CCA) The overall structure of CCA is similar to other class-II CCA-adding enzymes but significant differences occur in the body domain. Structural comparison of body and tail domains between CCA and other class-II CCA-adding enzymes unravels three specific regions of CCA. Based on the modeled CCA-tRNA complex, CCA may have a different tRNA binding pattern. The three specific regions located in the body domain of CCA also provide candidate regions for multi-targeted sorting. PubMed: 40519583DOI: 10.1016/j.yjsbx.2025.100127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.229 Å) |
Structure validation
Download full validation report
