1ltq: Difference between revisions

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[[Image:1ltq.gif|left|200px]]<br /><applet load="1ltq" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ltq.gif|left|200px]]
caption="1ltq, resolution 2.33&Aring;" />
 
'''CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE'''<br />
{{Structure
|PDB= 1ltq |SIZE=350|CAPTION= <scene name='initialview01'>1ltq</scene>, resolution 2.33&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=DMS:DIMETHYL SULFOXIDE'>DMS</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=
}}
 
'''CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE'''
 


==Overview==
==Overview==
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==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 <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].  
1LTQ 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=1LTQ OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12220496 12220496]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12220496 12220496]
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Polynucleotide 5'-hydroxy-kinase]]
[[Category: Polynucleotide 5'-hydroxy-kinase]]
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[[Category: phosphatase]]
[[Category: phosphatase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:20 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:05 2008''

Revision as of 10:35, 20 March 2008

File:1ltq.gif


Drag the structure with the mouse to rotate
1ltq, resolution 2.33Å
Ligands: ADP and DMS
Activity: Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78
Coordinates: save as pdb, mmCIF, xml



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. 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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