Open AccessCloning, expression, purification, crystallization and preliminary X‐ray analysis of peptidyl‐tRNA hydrolase from Mycobacterium tuberculosis
Author(s) -
Selvaraj M.,
Singh N. S.,
Roy Siddhartha,
Sangeetha R.,
Varshney Umesh,
Vijayan M.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106031125
Subject(s) - mycobacterium tuberculosis , transfer rna , enzyme , cleavage (geology) , ribosome , hydrolase , cloning (programming) , chemistry , escherichia coli , microbiology and biotechnology , stereochemistry , biology , biochemistry , tuberculosis , rna , gene , medicine , fracture (geology) , computer science , programming language , paleontology , pathology
Peptidyl‐tRNA hydrolase catalyses the cleavage of the ester link between the peptide and the tRNA in peptidyl‐tRNAs that, for various reasons, have dropped off the translating ribosomes. This enzyme from Mycobacterium tuberculosis has been crystallized in three related but distinct forms: P 2 1 2 1 2 1 , unit‐cell parameters a = 36.30, b = 61.85, c = 73.97 Å, P 2 1 , a = 35.83, b = 73.79, c = 59.79 Å, β = 92.3°, and P 2 1 2 1 2 1 , a = 35.84, b = 57.06, c = 72.59 Å. X‐ray data have been collected from all three forms.