1ltq
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(New page: 200px<br /><applet load="1ltq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ltq, resolution 2.33Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 18:45, 20 November 2007
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CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE
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 with ADP and DMS as ligands. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 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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