4P7B
Crystal structure of S. typhimurium peptidyl-tRNA hydrolase
4P7B の概要
| エントリーDOI | 10.2210/pdb4p7b/pdb |
| 分子名称 | Peptidyl-tRNA hydrolase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| 機能のキーワード | peptidyl-trna hydrolase peptidyl-trna recycling, hydrolase |
| 由来する生物種 | Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 |
| 細胞内の位置 | Cytoplasm (By similarity): D0ZJ57 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 44322.89 |
| 構造登録者 | Vandavasi, V.G.,McFeeters, R.L.,Taylor-Creel, K.,Coates, L.,McFeeters, H. (登録日: 2014-03-26, 公開日: 2014-07-09, 最終更新日: 2023-09-27) |
| 主引用文献 | Vandavasi, V.,Taylor-Creel, K.,McFeeters, R.L.,Coates, L.,McFeeters, H. Recombinant production, crystallization and X-ray crystallographic structure determination of peptidyl-tRNA hydrolase from Salmonella typhimurium. Acta Crystallogr.,Sect.F, 70:872-877, 2014 Cited by PubMed Abstract: Peptidyl-tRNA hydrolase (Pth; EC 3.1.1.29) from the pathogenic bacterium Salmonella typhimurium has been cloned, expressed in Escherichia coli and crystallized for X-ray analysis. Crystals were grown using hanging-drop vapor diffusion against a reservoir solution consisting of 0.03 M citric acid, 0.05 M bis-tris propane, 1% glycerol, 3% sucrose, 25% PEG 6000 pH 7.6. Crystals were used to obtain the three-dimensional structure of the native protein at 1.6 Å resolution. The structure was determined by molecular replacement of the crystallographic data processed in space group P2₁2₁2₁ with unit-cell parameters a=62.1, b=64.9, c=110.5 Å, α=β=γ=90°. The asymmetric unit of the crystallographic lattice was composed of two copies of the enzyme molecule with a 51% solvent fraction, corresponding to a Matthews coefficient of 2.02 Å3 Da(-1). The structural coordinates reported serve as a foundation for computational and structure-guided efforts towards novel small-molecule Pth1 inhibitors and potential antibacterial development. PubMed: 25005080DOI: 10.1107/S2053230X14009893 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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