1LTQ

CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE

Summary for 1LTQ

• Entry DOI: 10.2210/pdb1ltq/pdb
• Descriptor: POLYNUCLEOTIDE KINASE, ADENOSINE-5'-DIPHOSPHATE, DIMETHYL SULFOXIDE, ... (4 entities in total)
• Functional Keywords: kinase, phosphatase, alpha/beta, p-loop, transferase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 35739.93

Authors

Galburt, E.A.,Pelletier, J.,Wilson, G.,Stoddard, B.L. (deposition date: 2002-05-20, release date: 2002-10-09, Last modification date: 2024-10-09)

Primary citation

Galburt, E.A.,Pelletier, J.,Wilson, G.,Stoddard, B.L.
Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase.
Structure, 10:1249-1260, 2002

PubMed Abstract: 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.

PubMed: 12220496
DOI: 10.1016/S0969-2126(02)00835-3

Experimental method

X-RAY DIFFRACTION (2.33 Å)