6H42
crystal structure of the human TGT catalytic subunit QTRT1
Summary for 6H42
| Entry DOI | 10.2210/pdb6h42/pdb |
| Descriptor | Queuine tRNA-ribosyltransferase catalytic subunit 1, POTASSIUM ION, ZINC ION, ... (7 entities in total) |
| Functional Keywords | transglycosylase, queuine, trna, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 87261.65 |
| Authors | Johannsson, S.,Neumann, P.,Ficner, R. (deposition date: 2018-07-20, release date: 2018-09-05, Last modification date: 2024-06-19) |
| Primary citation | Johannsson, S.,Neumann, P.,Ficner, R. Crystal Structure of the Human tRNA Guanine Transglycosylase Catalytic Subunit QTRT1. Biomolecules, 8:-, 2018 Cited by PubMed Abstract: RNA modifications have been implicated in diverse and important roles in all kingdoms of life with over 100 of them present on tRNAs. A prominent modification at the wobble base of four tRNAs is the 7-deaza-guanine derivative queuine which substitutes the guanine at position 34. This exchange is catalyzed by members of the enzyme class of tRNA guanine transglycosylases (TGTs). These enzymes incorporate guanine substituents into tRNA, tRNA tRNA, and tRNA in all kingdoms of life. In contrast to the homodimeric bacterial TGT, the active eukaryotic TGT is a heterodimer in solution, comprised of a catalytic QTRT1 subunit and a noncatalytic QTRT2 subunit. Bacterial TGT enzymes, that incorporate a queuine precursor, have been identified or proposed as virulence factors for infections by pathogens in humans and therefore are valuable targets for drug design. To date no structure of a eukaryotic catalytic subunit is reported, and differences to its bacterial counterpart have to be deducted from sequence analysis and models. Here we report the first crystal structure of a eukaryotic QTRT1 subunit and compare it to known structures of the bacterial TGT and murine QTRT2. Furthermore, we were able to determine the crystal structure of QTRT1 in complex with the queuine substrate. PubMed: 30149595DOI: 10.3390/biom8030081 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
Download full validation report
