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

File:1rc8.gif


PDB ID 1rc8

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, resolution 2.75Å
Ligands: , and
Gene: PSET (Bacteriophage T4)
Activity: Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78
Coordinates: save as pdb, mmCIF, xml



OverviewOverview

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 StructureAbout this Structure

1RC8 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.

ReferenceReference

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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