1ly1: Difference between revisions
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'''Structure and Mechanism of T4 Polynucleotide Kinase''' | {{Structure | ||
|PDB= 1ly1 |SIZE=350|CAPTION= <scene name='initialview01'>1ly1</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Polynucleotide_5'-hydroxy-kinase Polynucleotide 5'-hydroxy-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.78 2.7.1.78] | |||
|GENE= PSET ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4]) | |||
}} | |||
'''Structure and Mechanism of T4 Polynucleotide Kinase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LY1 is a [ | 1LY1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY1 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12110598 12110598] | ||
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Polynucleotide 5'-hydroxy-kinase]] | [[Category: Polynucleotide 5'-hydroxy-kinase]] | ||
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[[Category: t4]] | [[Category: t4]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:36:33 2008'' | ||
Revision as of 10:36, 20 March 2008
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| 1ly1, resolution 2.00Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Gene: | PSET (Bacteriophage T4) | ||||||||||||
| Activity: | Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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