Role of methionine 71 in substrate recognition and structural integrity of bacterial peptidyl-tRNA hydrolase

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 carbo...

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Veröffentlicht in:	Biochimica et biophysica acta. Proteins and proteomics 2018-08, Vol.1866 (8), p.865-874
Hauptverfasser:	Shahid, Salman, Kabra, Ashish, Mundra, Surbhi, Pal, Ravi Kant, Tripathi, Sarita, Jain, Anupam, Arora, Ashish
Format:	Artikel
Sprache:	eng
Schlagworte:	Carboxylic Ester Hydrolases - genetics Carboxylic Ester Hydrolases - metabolism Catalytic Domain Crystallography, X-Ray Cytoplasm - metabolism Differential scanning calorimetry Hydrogen Bonding Magnetic Resonance Spectroscopy Methionine - metabolism Molecular Dynamics Simulation Molecular Structure NMR spectroscopy Peptidyl-tRNA hydrolase Protein Conformation Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Transfer, Amino Acyl - genetics RNA, Transfer, Amino Acyl - metabolism Substrate Specificity Vibrio cholerae - enzymology Vibrio cholerae - genetics
Online-Zugang:	Volltext
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