1ltq: Difference between revisions

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[[Image:1ltq.~~gif~~|left|200px]]

[[Image:1ltq.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE~~'''~~

===CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_12220496}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12220496 is the PubMed ID number.

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==About this Structure==

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[[Category: P-loop]]

[[Category: Phosphatase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:16:42 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:12:37 2008''

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-[[Image:1ltq.gif|left|200px]]
+{{Seed}}
+[[Image:1ltq.png|left|200px]]
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 {{STRUCTURE_1ltq|  PDB=1ltq  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF T4 POLYNUCLEOTIDE KINASE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12220496}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12220496 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12220496}}
 ==About this Structure==
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 [[Category: P-loop]]
 [[Category: Phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:16:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:12:37 2008''