4FYJ

Crystal Structure of P. aeruginosa peptidyl-tRNA hydrolase

Summary for 4FYJ

• Entry DOI: 10.2210/pdb4fyj/pdb
• Descriptor: Peptidyl-tRNA hydrolase (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cytoplasm : Q9HVC3
• Total number of polymer chains: 1
• Total formula weight: 21590.59

Authors

Hughes, R.C.,McFeeters, H.,McFeeters, R.L. (deposition date: 2012-07-04, release date: 2012-12-12, Last modification date: 2023-09-13)

Primary citation

Hughes, R.C.,McFeeters, H.,Coates, L.,McFeeters, R.L.
Recombinant production, crystallization and X-ray crystallographic structure determination of the peptidyl-tRNA hydrolase of Pseudomonas aeruginosa.
Acta Crystallogr.,Sect.F, 68:1472-1476, 2012

PubMed Abstract: The peptidyl-tRNA hydrolase enzyme from the pathogenic bacterium Pseudomonas aeruginosa (Pth; EC 3.1.1.29) has been cloned, expressed in Escherichia coli and crystallized for X-ray structural analysis. Suitable crystals were grown using the sitting-drop vapour-diffusion method after one week of incubation against a reservoir solution consisting of 20% polyethylene glycol 4000, 100 mM Tris pH 7.5, 10%(v/v) isopropyl alcohol. The crystals were used to obtain the three-dimensional structure of the native protein at 1.77 Å resolution. The structure was determined by molecular replacement of the crystallographic data processed in space group P6(1)22 with unit-cell parameters a=b=63.62, c=155.20 Å, α=β=90, γ=120°. The asymmetric unit of the crystallographic lattice was composed of a single copy of the enzyme molecule with a 43% solvent fraction, corresponding to a Matthews coefficient of 2.43 Å3 Da(-1). The crystallographic structure reported here will serve as the foundation for future structure-guided efforts towards the development of novel small-molecule inhibitors specific to bacterial Pths.

PubMed: 23192026
DOI: 10.1107/S1744309112045770

Experimental method

X-RAY DIFFRACTION (1.77 Å)