5we1: Difference between revisions
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<StructureSection load='5we1' size='340' side='right'caption='[[5we1]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='5we1' size='340' side='right'caption='[[5we1]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5we1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WE1 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5we1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WE1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.202Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5we1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5we1 OCA], [https://pdbe.org/5we1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5we1 RCSB], [https://www.ebi.ac.uk/pdbsum/5we1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5we1 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/POZ1_SCHPO POZ1_SCHPO] Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.<ref>PMID:18535244</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hu | [[Category: Schizosaccharomyces pombe 972h-]] | ||
[[Category: Huang | [[Category: Hu X]] | ||
[[Category: Kim | [[Category: Huang L]] | ||
[[Category: Komives | [[Category: Kim J-K]] | ||
[[Category: Liu | [[Category: Komives E-A]] | ||
[[Category: Qiao | [[Category: Liu J]] | ||
[[Category: Roskamp | [[Category: Qiao F]] | ||
[[Category: Sankaran | [[Category: Roskamp K]] | ||
[[Category: Yu | [[Category: Sankaran B]] | ||
[[Category: Yu C]] | |||
Latest revision as of 17:11, 4 October 2023
Structural Basis for Shelterin Bridge AssemblyStructural Basis for Shelterin Bridge Assembly
Structural highlights
FunctionPOZ1_SCHPO Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.[1] Publication Abstract from PubMedTelomere elongation through telomerase enables chromosome survival during cellular proliferation. The conserved multifunctional shelterin complex associates with telomeres to coordinate multiple telomere activities, including telomere elongation by telomerase. Similar to the human shelterin, fission yeast shelterin is composed of telomeric sequence-specific double- and single-stranded DNA-binding proteins, Taz1 and Pot1, respectively, bridged by Rap1, Poz1, and Tpz1. Here, we report the crystal structure of the fission yeast Tpz1(475-508)-Poz1-Rap1(467-496) complex that provides the structural basis for shelterin bridge assembly. Biochemical analyses reveal that shelterin bridge assembly is a hierarchical process in which Tpz1 binding to Poz1 elicits structural changes in Poz1, allosterically promoting Rap1 binding to Poz1. Perturbation of the cooperative Tpz1-Poz1-Rap1 assembly through mutation of the "conformational trigger" in Poz1 leads to unregulated telomere lengthening. Furthermore, we find that the human shelterin counterparts TPP1-TIN2-TRF2 also assemble hierarchically, indicating cooperativity as a conserved driving force for shelterin assembly. Structural Basis for Shelterin Bridge Assembly.,Kim JK, Liu J, Hu X, Yu C, Roskamp K, Sankaran B, Huang L, Komives EA, Qiao F Mol Cell. 2017 Nov 16;68(4):698-714.e5. doi: 10.1016/j.molcel.2017.10.032. PMID:29149597[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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