Summary for 5ZK0
| Entry DOI | 10.2210/pdb5zk0/pdb |
| Descriptor | Peptidyl-tRNA hydrolase, SODIUM ION (3 entities in total) |
| Functional Keywords | peptidyl-trna hydrolase, mutant m71a, hydrolase |
| Biological source | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Total number of polymer chains | 2 |
| Total formula weight | 43478.07 |
| Authors | Shahid, S.,Kabra, A.,Pal, R.K.,Arora, A. (deposition date: 2018-03-22, release date: 2018-06-06, Last modification date: 2024-10-16) |
| Primary citation | Shahid, S.,Kabra, A.,Mundra, S.,Pal, R.K.,Tripathi, S.,Jain, A.,Arora, A. Role of methionine 71 in substrate recognition and structural integrity of bacterial peptidyl-tRNA hydrolase. Biochim. Biophys. Acta, 1866:865-874, 2018 Cited by PubMed Abstract: Bacterial peptidyl-tRNA hydrolase (Pth) is an essential enzyme that alleviates tRNA starvation by recycling prematurely dissociated peptidyl-tRNAs. The specificity of Pth for N-blocked-aminoacyl-tRNA has been proposed to be contingent upon conserved residue N14 forming a hydrogen bond with the carbonyl of the first peptide bond in the substrate. M71 is involved in forming a conserved hydrogen bond with N14. Other interactions facilitating this recognition are not known. PubMed: 29733913DOI: 10.1016/j.bbapap.2018.05.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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