1ly1
From Proteopedia
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'''Structure and Mechanism of T4 Polynucleotide Kinase''' | '''Structure and Mechanism of T4 Polynucleotide Kinase''' | ||
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[[Category: Shuman, S.]] | [[Category: Shuman, S.]] | ||
[[Category: Wang, L K.]] | [[Category: Wang, L K.]] | ||
- | [[Category: | + | [[Category: Kinase]] |
- | [[Category: | + | [[Category: Phage]] |
- | [[Category: | + | [[Category: Phosphatase]] |
- | [[Category: | + | [[Category: Pnk]] |
- | [[Category: | + | [[Category: Polynucleotide]] |
- | [[Category: | + | [[Category: T4]] |
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 21:24, 2 May 2008
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 Enterobacteria phage t4. 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 Page seeded by OCA on Sat May 3 00:24:40 2008