Summary for 4YDU
| Entry DOI | 10.2210/pdb4ydu/pdb |
| Descriptor | tRNA N6-adenosine threonylcarbamoyltransferase, tRNA threonylcarbamoyladenosine biosynthesis protein TsaB, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total) |
| Functional Keywords | ygjd-yeaz complex, t6a transferase, transferase |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm : P05852 P76256 |
| Total number of polymer chains | 4 |
| Total formula weight | 128462.42 |
| Authors | Zhang, W.,Collinet, B.,Perrochia, L.,Durand, D.,Van Tilbeurgh, H. (deposition date: 2015-02-23, release date: 2015-03-04, Last modification date: 2024-11-13) |
| Primary citation | Zhang, W.,Collinet, B.,Perrochia, L.,Durand, D.,Van Tilbeurgh, H. The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli. Nucleic Acids Res., 43:1804-1817, 2015 Cited by PubMed Abstract: The essential and universal N(6)-threonylcarbamoyladenosine (t(6)A) modification at position 37 of ANN-decoding tRNAs plays a pivotal role in translational fidelity through enhancement of the cognate codon recognition and stabilization of the codon-anticodon interaction. In Escherichia coli, the YgjD (TsaD), YeaZ (TsaB), YjeE (TsaE) and YrdC (TsaC) proteins are necessary and sufficient for the in vitro biosynthesis of t(6)A, using tRNA, ATP, L-threonine and bicarbonate as substrates. YrdC synthesizes the short-lived L-threonylcarbamoyladenylate (TCA), and YgjD, YeaZ and YjeE cooperate to transfer the L-threonylcarbamoyl-moiety from TCA onto adenosine at position 37 of substrate tRNA. We determined the crystal structure of the heterodimer YgjD-YeaZ at 2.3 Å, revealing the presence of an unexpected molecule of ADP bound at an atypical site situated at the YgjD-YeaZ interface. We further showed that the ATPase activity of YjeE is strongly activated by the YgjD-YeaZ heterodimer. We established by binding experiments and SAXS data analysis that YgjD-YeaZ and YjeE form a compact ternary complex only in presence of ATP. The formation of the ternary YgjD-YeaZ-YjeE complex is required for the in vitro biosynthesis of t(6)A but not its ATPase activity. PubMed: 25578970DOI: 10.1093/nar/gku1397 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
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