1KEJ
Crystal Structure of Murine Terminal Deoxynucleotidyl Transferase complexed with ddATP
Summary for 1KEJ
| Entry DOI | 10.2210/pdb1kej/pdb |
| Related | 1BPY 1JMS 1KDH |
| Descriptor | Terminal deoxynucleotidyltransferase short isoform, COBALT (II) ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | polymerase, nucleotidyl transferase, pol x family, transferase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Isoform TDT-S: Nucleus. Isoform TDT-L: Cytoplasm: P09838 |
| Total number of polymer chains | 1 |
| Total formula weight | 42531.87 |
| Authors | Delarue, M.,Boule, J.B.,Lescar, J.,Expert-Bezancon, N.,Jourdan, N.,Sukumar, N.,Rougeon, F.,Papanicolaou, C. (deposition date: 2001-11-16, release date: 2002-05-16, Last modification date: 2023-08-16) |
| Primary citation | Delarue, M.,Boule, J.B.,Lescar, J.,Expert-Bezancon, N.,Jourdan, N.,Sukumar, N.,Rougeon, F.,Papanicolaou, C. Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase. EMBO J., 21:427-439, 2002 Cited by PubMed Abstract: The crystal structure of the catalytic core of murine terminal deoxynucleotidyltransferase (TdT) at 2.35 A resolution reveals a typical DNA polymerase beta-like fold locked in a closed form. In addition, the structures of two different binary complexes, one with an oligonucleotide primer and the other with an incoming ddATP-Co(2+) complex, show that the substrates and the two divalent ions in the catalytic site are positioned in TdT in a manner similar to that described for the human DNA polymerase beta ternary complex, suggesting a common two metal ions mechanism of nucleotidyl transfer in these two proteins. The inability of TdT to accommodate a template strand can be explained by steric hindrance at the catalytic site caused by a long lariat-like loop, which is absent in DNA polymerase beta. However, displacement of this discriminating loop would be sufficient to unmask a number of evolutionarily conserved residues, which could then interact with a template DNA strand. The present structure can be used to model the recently discovered human polymerase mu, with which it shares 43% sequence identity. PubMed: 11823435DOI: 10.1093/emboj/21.3.427 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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