4RR6
N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA (snapshot 1)
Summary for 4RR6
| Entry DOI | 10.2210/pdb4rr6/pdb |
| Related | 4RR7 4RR8 4RR9 4RRA 4RRB 4RRC 4RRD 4RRF 4RRG 4RRH 4RRI 4RRJ 4RRK 4RRL 4RRM 4RRQ 4RRR |
| Descriptor | Probable threonine--tRNA ligase 2, SERINE-3'-AMINOADENOSINE (3 entities in total) |
| Functional Keywords | dtd-like, proofreading, ligase |
| Biological source | Aeropyrum pernix K1 |
| Cellular location | Cytoplasm : Q9YFY3 |
| Total number of polymer chains | 1 |
| Total formula weight | 15488.75 |
| Authors | Ahmad, S.,Muthukumar, S.,Yerabham, A.S.K.,Kamarthapu, V.,Sankaranarayanan, R. (deposition date: 2014-11-06, release date: 2015-07-15, Last modification date: 2024-02-28) |
| Primary citation | Ahmad, S.,Muthukumar, S.,Kuncha, S.K.,Routh, S.B.,Yerabham, A.S.,Hussain, T.,Kamarthapu, V.,Kruparani, S.P.,Sankaranarayanan, R. Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme. Nat Commun, 6:7552-7552, 2015 Cited by PubMed Abstract: Proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. Here, we show that a unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes. We show, using three distinct archaea, that a side-chain-stripped recognition site is fully capable of solving a subtle discrimination problem. While biochemical probing establishes that RNA plays the catalytic role, mechanistic insights from multiple high-resolution snapshots reveal that differential remodelling of the catalytic core at the RNA-peptide interface provides the determinants for correct proofreading activity. The functional crosstalk between RNA and protein elucidated here suggests how primordial enzyme functions could have emerged on RNA-peptide scaffolds before recruitment of specific side chains. PubMed: 26113036DOI: 10.1038/ncomms8552 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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