2NAF

Solution structure of peptidyl-tRNA hydrolase from Mycobacterium smegmatis

Summary for 2NAF

• Entry DOI: 10.2210/pdb2naf/pdb
• Descriptor: Peptidyl-tRNA hydrolase (1 entity in total)
• Functional Keywords: protein, hydrolase
• Biological source: Mycobacterium smegmatis str. MC2 155
• Cellular location: Cytoplasm : A0R3D3
• Total number of polymer chains: 1
• Total formula weight: 20306.32

Authors

Yadav, R.,Pathak, P.,Fatma, F.,Kabra, A.,Pulavarti, S.,Jain, A.,Kumar, A.,Shukla, V.,Arora, A. (deposition date: 2015-12-23, release date: 2017-01-11, Last modification date: 2024-05-15)

Primary citation

Kabra, A.,Fatma, F.,Shahid, S.,Pathak, P.P.,Yadav, R.,Pulavarti, S.V.,Tripathi, S.,Jain, A.,Arora, A.
Structural characterization of peptidyl-tRNA hydrolase from Mycobacterium smegmatis by NMR spectroscopy.
Biochim.Biophys.Acta, 1864:1304-1314, 2016

PubMed Abstract: Accumulation of toxic peptidyl-tRNAs in the bacterial cytoplasm is averted by the action of peptidyl-tRNA hydrolase (Pth), which cleaves peptidyl-tRNA into free tRNA and peptide. NMR studies are needed for a protein homolog with a complete crystal structure, for comparison with the NMR structure of Mycobacterium tuberculosis Pth.

PubMed: 27378575
DOI: 10.1016/j.bbapap.2016.06.013

Experimental method

SOLUTION NMR