1ly1

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Revision as of 18:51, 20 November 2007

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spinqualitylabelsall models 1ly1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure and Mechanism of T4 Polynucleotide Kinase

Overview

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.

About this Structure

1LY1 is a Single protein structure of sequence from Bacteriophage t4 with SO4 as ligand. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 Full crystallographic information is available from OCA.

Reference

Structure and mechanism of T4 polynucleotide kinase: an RNA repair enzyme., Wang LK, Lima CD, Shuman S, EMBO J. 2002 Jul 15;21(14):3873-80. PMID:12110598

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