Open AccessStructures of new crystal forms of Mycobacterium tuberculosis peptidyl‐tRNA hydrolase and functionally important plasticity of the molecule
Author(s) -
Selvaraj M.,
Ahmad Rais,
Varshney Umesh,
Vijayan M.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111052341
Subject(s) - hydrolase , molecule , transfer rna , stereochemistry , chemistry , crystal structure , crystallography , enzyme , binding site , mycobacterium tuberculosis , peptide , biochemistry , rna , tuberculosis , organic chemistry , gene , medicine , pathology
The X‐ray structures of new crystal forms of peptidyl‐tRNA hydrolase from M. tuberculosis reported here and the results of previous X‐ray studies of the enzyme from different sources provide a picture of the functionally relevant plasticity of the protein molecule. The new X‐ray results confirm the connection deduced previously between the closure of the lid at the peptide‐binding site and the opening of the gate that separates the peptide‐binding and tRNA‐binding sites. The plasticity of the molecule indicated by X‐ray structures is in general agreement with that deduced from the available solution NMR results. The correlation between the lid and the gate movements is not, however, observed in the NMR structure.