1ltq
From Proteopedia
(New page: 200px<br /><applet load="1ltq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ltq, resolution 2.33Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ltq.gif|left|200px]]<br /><applet load="1ltq" size=" | + | [[Image:1ltq.gif|left|200px]]<br /><applet load="1ltq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ltq, resolution 2.33Å" /> | caption="1ltq, resolution 2.33Å" /> | ||
'''CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE'''<br /> | '''CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | T4 phage polynucleotide kinase (PNK) was identified over 35 years ago and | + | T4 phage polynucleotide kinase (PNK) was identified over 35 years ago and has become a staple reagent for molecular biologists. The enzyme displays 5'-hydroxyl kinase, 3'-phosphatase, and 2',3'-cyclic phosphodiesterase activities against a wide range of substrates. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase. DNA repair enzymes that share conserved motifs with PNK have been identified in eukaryotes. PNK contains two functionally distinct structural domains and forms a homotetramer. The C-terminal phosphatase domain is homologous to the L-2-haloacid dehalogenase family and the N-terminal kinase domain is homologous to adenylate kinase. The active sites have been characterized through structural homology analyses and visualization of bound substrate. |
==About this Structure== | ==About this Structure== | ||
| - | 1LTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with ADP and DMS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1LTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=DMS:'>DMS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Polynucleotide 5'-hydroxy-kinase]] | [[Category: Polynucleotide 5'-hydroxy-kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Galburt, E | + | [[Category: Galburt, E A.]] |
[[Category: Pelletier, J.]] | [[Category: Pelletier, J.]] | ||
| - | [[Category: Stoddard, B | + | [[Category: Stoddard, B L.]] |
[[Category: Wilson, G.]] | [[Category: Wilson, G.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: phosphatase]] | [[Category: phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:20 2008'' |
Revision as of 11:48, 21 February 2008
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CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE
Overview
T4 phage polynucleotide kinase (PNK) was identified over 35 years ago and has become a staple reagent for molecular biologists. The enzyme displays 5'-hydroxyl kinase, 3'-phosphatase, and 2',3'-cyclic phosphodiesterase activities against a wide range of substrates. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase. DNA repair enzymes that share conserved motifs with PNK have been identified in eukaryotes. PNK contains two functionally distinct structural domains and forms a homotetramer. The C-terminal phosphatase domain is homologous to the L-2-haloacid dehalogenase family and the N-terminal kinase domain is homologous to adenylate kinase. The active sites have been characterized through structural homology analyses and visualization of bound substrate.
About this Structure
1LTQ is a Single protein structure of sequence from Bacteriophage t4 with and as ligands. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 Full crystallographic information is available from OCA.
Reference
Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase., Galburt EA, Pelletier J, Wilson G, Stoddard BL, Structure. 2002 Sep;10(9):1249-60. PMID:12220496
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