4P7B

Crystal structure of S. typhimurium peptidyl-tRNA hydrolase

Summary for 4P7B

• Entry DOI: 10.2210/pdb4p7b/pdb
• Descriptor: Peptidyl-tRNA hydrolase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: peptidyl-trna hydrolase peptidyl-trna recycling, hydrolase
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
• Cellular location: Cytoplasm (By similarity): D0ZJ57
• Total number of polymer chains: 2
• Total formula weight: 44322.89

Authors

Vandavasi, V.G.,McFeeters, R.L.,Taylor-Creel, K.,Coates, L.,McFeeters, H. (deposition date: 2014-03-26, release date: 2014-07-09, Last modification date: 2023-09-27)

Primary citation

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

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: 25005080
DOI: 10.1107/S2053230X14009893

Experimental method

X-RAY DIFFRACTION (1.6 Å)