3TCK: Crystal Structure Of Peptidyl-Trna Hydrolase From Mycobacterium Tuberculosis - Form 4

Citation:
Abstract
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.
PDB ID: 3TCKDownload
MMDB ID: 97272
PDB Deposition Date: 2011/8/9
Updated in MMDB: 2012/02
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 3TCK: monomeric; determined by author and by software (PISA)
Molecular Components in 3TCK
Label Count Molecule
Protein (1 molecule)
1
Peptidyl-trna Hydrolase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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