1rc8

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spinqualitylabelsall models 1rc8, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

T4 Polynucleotide Kinase bound to 5'-GTCAC-3' ssDNA

Overview

T4 phage polynucleotide kinase (PNK) displays 5'-hydroxyl kinase, 3'-phosphatase and 2',3'-cyclic phosphodiesterase activities. The enzyme, phosphorylates the 5' hydroxyl termini of a wide variety of nucleic acid, substrates, a behavior studied here through the determination of a series, of crystal structures with single-stranded (ss)DNA oligonucleotide, substrates of various lengths and sequences. In these structures, the 5', ribose hydroxyl is buried in the kinase active site in proper alignment, for phosphoryl transfer. Depending on the ssDNA length, the first two or, three nucleotide bases are well ordered. Numerous contacts are made both, to the phosphoribosyl backbone and to the ordered bases. The position, side chain contacts and internucleotide stacking interactions of the, ordered bases are strikingly different for a 5'-GT DNA end than for a, 5'-TG end. The base preferences displayed at those positions by PNK are, attributable to differences in the enzyme binding interactions and in the, DNA conformation for each unique substrate molecule.

About this Structure

1RC8 is a Single protein structure of sequence from Bacteriophage t4 with CA, DMS and ADP as ligands. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 Full crystallographic information is available from OCA.

Reference

Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase., Eastberg JH, Pelletier J, Stoddard BL, Nucleic Acids Res. 2004 Jan 30;32(2):653-60. Print 2004. PMID:14754987

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