1ltq | pdb_00001ltq
CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE
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| 1ltq, resolution 2.33Å | |||||||||||||
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| Ligands: | ADP and DMS | ||||||||||||
| Activity: | Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1LTQ is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase., Galburt EA, Pelletier J, Wilson G, Stoddard BL, Structure. 2002 Sep;10(9):1249-60. PMID:12220496
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