1LY1

Structure and Mechanism of T4 Polynucleotide Kinase

Summary for 1LY1

• Entry DOI: 10.2210/pdb1ly1/pdb
• Descriptor: polynucleotide kinase, SULFATE ION (3 entities in total)
• Functional Keywords: pnk, kinase, phosphatase, polynucleotide, t4, phage, transferase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 21055.04

Authors

Wang, L.K.,Lima, C.D.,Shuman, S. (deposition date: 2002-06-06, release date: 2002-07-17, Last modification date: 2024-02-14)

Primary citation

Wang, L.K.,Lima, C.D.,Shuman, S.
Structure and mechanism of T4 polynucleotide kinase: an RNA repair enzyme.
EMBO J., 21:3873-3880, 2002

PubMed Abstract: T4 polynucleotide kinase (Pnk), in addition to being an invaluable research tool, exemplifies a family of bifunctional enzymes with 5'-kinase and 3'-phosphatase activities that play key roles in RNA and DNA repair. T4 Pnk is a homotetramer composed of a C-terminal phosphatase domain and an N-terminal kinase domain. The 2.0 A crystal structure of the isolated kinase domain highlights a tunnel-like active site through the heart of the enzyme, with an entrance on the 5' OH acceptor side that can accommodate a single-stranded polynucleotide. The active site is composed of essential side chains that coordinate the beta phosphate of the NTP donor and the 3' phosphate of the 5' OH acceptor, plus a putative general acid that activates the 5' OH. The structure rationalizes the different specificities of T4 and eukaryotic Pnk and suggests a model for the assembly of the tetramer.

PubMed: 12110598
DOI: 10.1093/emboj/cdf397

Experimental method

X-RAY DIFFRACTION (2 Å)