1yjm
From Proteopedia
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| - | [[ | + | ==Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.== |
| + | <StructureSection load='1yjm' size='340' side='right' caption='[[1yjm]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1yjm]] is a 6 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YJM FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yj5|1yj5]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_5'-hydroxyl-kinase Polynucleotide 5'-hydroxyl-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.78 2.7.1.78] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1yjm RCSB], [http://www.ebi.ac.uk/pdbsum/1yjm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PNKP_MOUSE PNKP_MOUSE]] Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yj/1yjm_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:15749016</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Polynucleotide 5'-hydroxyl-kinase]] | [[Category: Polynucleotide 5'-hydroxyl-kinase]] | ||
| - | [[Category: Bernstein, N K | + | [[Category: Bernstein, N K]] |
| - | [[Category: Cass, C E | + | [[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 N.M | + | [[Category: Glover, J N.M]] |
| - | [[Category: Green, R | + | [[Category: Green, R]] |
| - | [[Category: Karimi-Busheri, F | + | [[Category: Karimi-Busheri, F]] |
| - | [[Category: Koch, C A | + | [[Category: Koch, C A]] |
| - | [[Category: Mani, R S | + | [[Category: Mani, R S]] |
| - | [[Category: Rakovszky, M L | + | [[Category: Rakovszky, M L]] |
| - | [[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: Transferase-dna binding protein complex]] | [[Category: Transferase-dna binding protein complex]] | ||
[[Category: Xrcc4 phosphopeptide]] | [[Category: Xrcc4 phosphopeptide]] | ||
Revision as of 02:08, 25 December 2014
Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.
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Categories: Mus musculus | Polynucleotide 5'-hydroxyl-kinase | 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 | Fha domain | Polynucleotide kinase | Transferase-dna binding protein complex | Xrcc4 phosphopeptide
