1yjm

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[[Image:1yjm.gif|left|200px]]<br /><applet load="1yjm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yjm.gif|left|200px]]
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caption="1yjm, resolution 2.20&Aring;" />
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'''Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.'''<br />
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{{Structure
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|PDB= 1yjm |SIZE=350|CAPTION= <scene name='initialview01'>1yjm</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|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]
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|GENE= Pnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ACE:'>ACE</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=1YJM OCA].
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1YJM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJM OCA].
==Reference==
==Reference==
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The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase., Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN, Mol Cell. 2005 Mar 4;17(5):657-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15749016 15749016]
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The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase., Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN, Mol Cell. 2005 Mar 4;17(5):657-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15749016 15749016]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Polynucleotide 5'-hydroxy-kinase]]
[[Category: Polynucleotide 5'-hydroxy-kinase]]
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[[Category: xrcc4 phosphopeptide]]
[[Category: xrcc4 phosphopeptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:46 2008''

Revision as of 13:23, 20 March 2008

Image:1yjm.gif


PDB ID 1yjm

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Gene: Pnk (Mus musculus)
Activity: Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.


Overview

Mammalian polynucleotide kinase (PNK) is a key component of both the base excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways. PNK acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. PNK is recruited to repair complexes through interactions between its N-terminal FHA domain and phosphorylated components of either pathway. Here, we describe the crystal structure of intact mammalian PNK and a structure of the PNK FHA bound to a cognate phosphopeptide. The kinase domain has a broad substrate binding pocket, which preferentially recognizes double-stranded substrates with recessed 5' termini. In contrast, the phosphatase domain efficiently dephosphorylates single-stranded 3'-phospho termini as well as double-stranded substrates. The FHA domain is linked to the kinase/phosphatase catalytic domain by a flexible tether, and it exhibits a mode of target selection based on electrostatic complementarity between the binding surface and the phosphothreonine peptide.

About this Structure

1YJM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase., Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN, Mol Cell. 2005 Mar 4;17(5):657-70. PMID:15749016

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