1LTQ: Crystal Structure Of T4 Polynucleotide Kinase

T4 phage polynucleotide kinase (PNK) was identified over 35 years ago and has become a staple reagent for molecular biologists. The enzyme displays 5'-hydroxyl kinase, 3'-phosphatase, and 2',3'-cyclic phosphodiesterase activities against a wide range of substrates. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase. DNA repair enzymes that share conserved motifs with PNK have been identified in eukaryotes. PNK contains two functionally distinct structural domains and forms a homotetramer. The C-terminal phosphatase domain is homologous to the L-2-haloacid dehalogenase family and the N-terminal kinase domain is homologous to adenylate kinase. The active sites have been characterized through structural homology analyses and visualization of bound substrate.
PDB ID: 1LTQDownload
MMDB ID: 20925
PDB Deposition Date: 2002/5/20
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.33  Å
Source Organism:
Similar Structures:
Biological Unit for 1LTQ: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1LTQ
Label Count Molecule
Proteins (4 molecules)
Polynucleotide Kinase(Gene symbol: pseT)
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

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