1yjm
From Proteopedia
(New page: 200px<br /><applet load="1yjm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yjm, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1yjm.gif|left|200px]]<br /><applet load="1yjm" size=" | + | [[Image:1yjm.gif|left|200px]]<br /><applet load="1yjm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yjm, resolution 2.20Å" /> | caption="1yjm, resolution 2.20Å" /> | ||
'''Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.'''<br /> | '''Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mammalian polynucleotide kinase (PNK) is a key component of both the base | + | 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== | ==About this Structure== | ||
| - | 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 ACE 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Polynucleotide 5'-hydroxy-kinase]] | [[Category: Polynucleotide 5'-hydroxy-kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bernstein, N | + | [[Category: Bernstein, N K.]] |
| - | [[Category: Cass, C | + | [[Category: Cass, C E.]] |
[[Category: Cui, D.]] | [[Category: Cui, D.]] | ||
[[Category: Durocher, D.]] | [[Category: Durocher, D.]] | ||
[[Category: Galicia, S.]] | [[Category: Galicia, S.]] | ||
| - | [[Category: Glover, J | + | [[Category: Glover, J N.M.]] |
[[Category: Green, R.]] | [[Category: Green, R.]] | ||
[[Category: Karimi-Busheri, F.]] | [[Category: Karimi-Busheri, F.]] | ||
| - | [[Category: Koch, C | + | [[Category: Koch, C A.]] |
| - | [[Category: Mani, R | + | [[Category: Mani, R S.]] |
| - | [[Category: Rakovszky, M | + | [[Category: Rakovszky, M L.]] |
[[Category: Weinfeld, M.]] | [[Category: Weinfeld, M.]] | ||
| - | [[Category: Williams, R | + | [[Category: Williams, R S.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: fha domain]] | [[Category: fha domain]] | ||
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[[Category: xrcc4 phosphopeptide]] | [[Category: xrcc4 phosphopeptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:00 2008'' |
Revision as of 14:06, 21 February 2008
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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 with as ligand. Active as Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 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
Page seeded by OCA on Thu Feb 21 16:06:00 2008
Categories: Mus musculus | Polynucleotide 5'-hydroxy-kinase | Single protein | Bernstein, N K. | Cass, C E. | Cui, D. | Durocher, D. | Galicia, S. | Glover, J N.M. | Green, R. | Karimi-Busheri, F. | Koch, C A. | Mani, R S. | Rakovszky, M L. | Weinfeld, M. | Williams, R S. | ACE | Fha domain | Polynucleotide kinase | Xrcc4 phosphopeptide
