3NEA
Crystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensis
Summary for 3NEA
| Entry DOI | 10.2210/pdb3nea/pdb |
| Descriptor | Peptidyl-tRNA hydrolase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | hydrolase, peptidyl-trna |
| Biological source | Francisella tularensis subsp. tularensis |
| Cellular location | Cytoplasm : Q5NGZ6 |
| Total number of polymer chains | 1 |
| Total formula weight | 23184.76 |
| Authors | Lam, R.,McGrath, T.E.,Romanov, V.,Gothe, S.A.,Peddi, S.R.,Razumova, E.,Lipman, R.S.,Branstrom, A.A.,Chirgadze, N.Y. (deposition date: 2010-06-08, release date: 2011-06-15, Last modification date: 2023-09-06) |
| Primary citation | Clarke, T.E.,Romanov, V.,Lam, R.,Gothe, S.A.,Peddi, S.R.,Razumova, E.B.,Lipman, R.S.,Branstrom, A.A.,Chirgadze, N.Y. Structure of Francisella tularensis peptidyl-tRNA hydrolase. Acta Crystallogr.,Sect.F, 67:446-449, 2011 Cited by PubMed Abstract: The rational design of novel antibiotics for bacteria involves the identification of inhibitors for enzymes involved in essential biochemical pathways in cells. In this study, the cloning, expression, purification, crystallization and structure of the enzyme peptidyl-tRNA hydrolase from Francisella tularensis, the causative agent of tularemia, was performed. The structure of F. tularensis peptidyl-tRNA hydrolase is comparable to those of other bacterial peptidyl-tRNA hydrolases, with most residues in the active site conserved amongst the family. The resultant reagents, structural data and analyses provide essential information for the structure-based design of novel inhibitors for this class of proteins. PubMed: 21505237DOI: 10.1107/S174430911100515X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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