3H38
The structure of CCA-adding enzyme apo form II
Summary for 3H38
| Entry DOI | 10.2210/pdb3h38/pdb |
| Related | 3H37 3H39 3H3A |
| Descriptor | TRNA nucleotidyl transferase-related protein (2 entities in total) |
| Functional Keywords | transferase/rna, nucleotide-binding, nucleotidyltransferase, rna-binding, transferase |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 1 |
| Total formula weight | 51530.62 |
| Authors | Toh, Y.,Tomita, K. (deposition date: 2009-04-16, release date: 2009-10-13, Last modification date: 2023-11-01) |
| Primary citation | Toh, Y.,Takeshita, D.,Numata, T.,Fukai, S.,Nureki, O.,Tomita, K. Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme Embo J., 28:3353-3365, 2009 Cited by PubMed Abstract: The CCA-adding enzyme synthesizes the CCA sequence at the 3' end of tRNA without a nucleic acid template. The crystal structures of class II Thermotoga maritima CCA-adding enzyme and its complexes with CTP or ATP were determined. The structure-based replacement of both the catalytic heads and nucleobase-interacting neck domains of the phylogenetically closely related Aquifex aeolicus A-adding enzyme by the corresponding domains of the T. maritima CCA-adding enzyme allowed the A-adding enzyme to add CCA in vivo and in vitro. However, the replacement of only the catalytic head domain did not allow the A-adding enzyme to add CCA, and the enzyme exhibited (A, C)-adding activity. We identified the region in the neck domain that prevents (A, C)-adding activity and defines the number of nucleotide incorporations and the specificity for correct CCA addition. We also identified the region in the head domain that defines the terminal A addition after CC addition. The results collectively suggest that, in the class II CCA-adding enzyme, the head and neck domains collaboratively and dynamically define the number of nucleotide additions and the specificity of nucleotide selection. PubMed: 19745807DOI: 10.1038/emboj.2009.260 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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