1ly1

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(New page: 200px<br /><applet load="1ly1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ly1, resolution 2.00&Aring;" /> '''Structure and Mechan...)
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caption="1ly1, resolution 2.00&Aring;" />
'''Structure and Mechanism of T4 Polynucleotide Kinase'''<br />
'''Structure and Mechanism of T4 Polynucleotide Kinase'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1LY1 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LY1 OCA].
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1LY1 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1LY1 OCA].
==Reference==
==Reference==
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[[Category: Polynucleotide 5'-hydroxy-kinase]]
[[Category: Polynucleotide 5'-hydroxy-kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lima, C.D.]]
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[[Category: Lima, C D.]]
[[Category: Shuman, S.]]
[[Category: Shuman, S.]]
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[[Category: Wang, L.K.]]
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[[Category: Wang, L K.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: kinase]]
[[Category: kinase]]
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[[Category: t4]]
[[Category: t4]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:58:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:28 2008''

Revision as of 11:49, 21 February 2008


1ly1, resolution 2.00Å

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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 with as ligand. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 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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