7YLL
Crystal structure of TTEDbh
Summary for 7YLL
| Entry DOI | 10.2210/pdb7yll/pdb |
| Descriptor | DNA polymerase IV, PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | polymerase of dinb subfamily, translesion synthesis, dna binding protein, replication, transferase |
| Biological source | Thermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) |
| Total number of polymer chains | 1 |
| Total formula weight | 44107.54 |
| Authors | |
| Primary citation | Tian, L.F.,Gao, H.,Yang, S.,Liu, Y.P.,Li, M.,Xu, W.,Yan, X.X. Structure and function of extreme TLS DNA polymerase TTEDbh from Thermoanaerobacter tengcongensis. Int.J.Biol.Macromol., 253:126770-126770, 2023 Cited by PubMed Abstract: Translesion synthesis (TLS) is a kind of DNA repair that maintains the stability of the genome and ensures the normal growth of life in cells under emergencies. Y-family DNA polymerases, as a kind of error-prone DNA polymerase, mainly perform TLS. Previous studies have suggested that the occurrence of tumors is associated with the overexpression of human DNA polymerase of the Y family. And the combination of Y-family DNA polymerase inhibitors is promising for cancer therapy. Here we report the functional and structural characterization of a member of the Y-family DNA polymerases, TTEDbh. We determine TTEDbh is an extreme TLS polymerase that can cross oxidative damage sites, and further identify the amino acids and novel structures that are critical for DNA binding, synthesis, fidelity, and oxidative damage bypass. Moreover, previously unnoticed structural elements with important functions have been discovered and analyzed. These studies provide a more experimental basis for further elucidating the molecular mechanisms of DNA polymerase in the Y family. It could also shed light on the design of drugs to target tumors. PubMed: 37683741DOI: 10.1016/j.ijbiomac.2023.126770 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.60000921196 Å) |
Structure validation
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