1yjm: Difference between revisions
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|PDB= 1yjm |SIZE=350|CAPTION= <scene name='initialview01'>1yjm</scene>, resolution 2.20Å | |PDB= 1yjm |SIZE=350|CAPTION= <scene name='initialview01'>1yjm</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= Pnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Pnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1yj5|1YJ5]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjm OCA], [http://www.ebi.ac.uk/pdbsum/1yjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yjm RCSB]</span> | |||
}} | }} | ||
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[[Category: Weinfeld, M.]] | [[Category: Weinfeld, M.]] | ||
[[Category: Williams, R S.]] | [[Category: Williams, R S.]] | ||
[[Category: fha domain]] | [[Category: fha domain]] | ||
[[Category: polynucleotide kinase]] | [[Category: polynucleotide kinase]] | ||
[[Category: xrcc4 phosphopeptide]] | [[Category: xrcc4 phosphopeptide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:09:46 2008'' | ||
Revision as of 22:09, 30 March 2008
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| 1yjm, resolution 2.20Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ACE, TPO | ||||||||||||
| Gene: | Pnk (Mus musculus) | ||||||||||||
| Activity: | Polynucleotide 5'-hydroxy-kinase, with EC number 2.7.1.78 | ||||||||||||
| Related: | 1YJ5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| 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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