3TD6

Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis from trigonal partially dehydrated crystal

Summary for 3TD6

• Entry DOI: 10.2210/pdb3td6/pdb
• Related: 2JRC 2PTH 2Z2I 2Z2J 2Z2K 3P2J 3TCK 3TCN 3TD2
• Descriptor: Peptidyl-tRNA hydrolase (2 entities in total)
• Functional Keywords: pth, hydrolysis of peptidyl-trna, peptidyl-trna, cytosol, hydrolase
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (By similarity): P65865
• Total number of polymer chains: 1
• Total formula weight: 20485.53

Authors

Selvaraj, M.,Ahmad, R.,Varshney, U.,Vijayan, M. (deposition date: 2011-08-10, release date: 2012-02-15, Last modification date: 2023-11-01)

Primary citation

Selvaraj, M.,Ahmad, R.,Varshney, U.,Vijayan, M.
Structures of new crystal forms of Mycobacterium tuberculosis peptidyl-tRNA hydrolase and functionally important plasticity of the molecule
Acta Crystallogr.,Sect.F, 68:124-128, 2012

PubMed 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.

PubMed: 22297982
DOI: 10.1107/S1744309111052341

Experimental method

X-RAY DIFFRACTION (3.2 Å)