1yj5

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[[Image:1yj5.gif|left|200px]]
[[Image:1yj5.gif|left|200px]]
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{{Structure
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|PDB= 1yj5 |SIZE=350|CAPTION= <scene name='initialview01'>1yj5</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1yj5", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1yj5| PDB=1yj5 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yj5 OCA], [http://www.ebi.ac.uk/pdbsum/1yj5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yj5 RCSB]</span>
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'''Molecular architecture of mammalian polynucleotide kinase, a DNA repair enzyme'''
'''Molecular architecture of mammalian polynucleotide kinase, a DNA repair enzyme'''
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[[Category: Weinfeld, M.]]
[[Category: Weinfeld, M.]]
[[Category: Williams, R S.]]
[[Category: Williams, R S.]]
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[[Category: beta sandwich]]
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[[Category: Beta sandwich]]
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[[Category: p-loop]]
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[[Category: P-loop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:23:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:09:10 2008''
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Revision as of 13:23, 3 May 2008

Image:1yj5.gif

Template:STRUCTURE 1yj5

Molecular architecture of mammalian polynucleotide kinase, a DNA repair enzyme


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

1YJ5 is a Protein complex structure of sequences 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 Page seeded by OCA on Sat May 3 16:23:08 2008

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