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==Crystal structure of Ku80 and Sir4==
==Crystal structure of Ku80 and Sir4==
<StructureSection load='5y59' size='340' side='right' caption='[[5y59]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='5y59' size='340' side='right'caption='[[5y59]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_VL3 Saccharomyces cerevisiae VL3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.402&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5y58|5y58]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [https://pdbe.org/5y59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [https://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</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=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [http://pdbe.org/5y59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [http://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>
[https://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>  
 
==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA helicase]]
[[Category: Large Structures]]
[[Category: Chen, H]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Lei, M]]
[[Category: Saccharomyces cerevisiae VL3]]
[[Category: Wu, J]]
[[Category: Chen H]]
[[Category: Xue, J]]
[[Category: Lei M]]
[[Category: Protein binding]]
[[Category: Wu J]]
[[Category: Protein-protein complex]]
[[Category: Xue J]]
[[Category: Telomerase]]
[[Category: Telomere]]

Latest revision as of 10:21, 27 March 2024

Crystal structure of Ku80 and Sir4

5y59, resolution 2.40Å

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