5we0: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Joel L. Sussman

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-'''Unreleased structure'''
-The entry 5we0 is ON HOLD  until Paper Publication
+==Structural Basis for Shelterin Bridge Assembly==
+<StructureSection load='5we0' size='340' side='right'caption='[[5we0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5we0]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WE0 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">poz1, SPAC19G12.13c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), tpz1, mug169, SPAC6F6.16c, SPAC6F6.18c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), rap1, SPBC1778.02 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=5we0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5we0 OCA], [http://pdbe.org/5we0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5we0 RCSB], [http://www.ebi.ac.uk/pdbsum/5we0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5we0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/POZ1_SCHPO POZ1_SCHPO]] Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.<ref>PMID:18535244</ref>  [[http://www.uniprot.org/uniprot/RAP1_SCHPO RAP1_SCHPO]] Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE). Unlike yeast, exhibits no effect in transcription regulation.<ref>PMID:11676924</ref> <ref>PMID:11676925</ref> <ref>PMID:19948484</ref>  [[http://www.uniprot.org/uniprot/TPZ1_SCHPO TPZ1_SCHPO]] Telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang and involved in telomere length regulation. recruits poz1 and ccq1 to telomeres, regulating telomere length negatively and positivels respectively.<ref>PMID:16303567</ref> <ref>PMID:18535244</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Telomere 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.
-Authors: Kim, J.-K., Liu, J., Hu, X., Sankaran, B., Qiao, F.
+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<ref>PMID:29149597</ref>
-Description: Structural Basis for Telomere Length Regulation by the Shelterin Bridge
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5we0" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Fission yeast]]
+[[Category: Large Structures]]
+[[Category: Hu, X]]
+[[Category: Huang, L]]
+[[Category: Kim, J K]]
+[[Category: Komives, E A]]
+[[Category: Liu, J]]
 [[Category: Qiao, F]]
+[[Category: Roskamp, K]]
 [[Category: Sankaran, B]]
-[[Category: Kim, J.-K]]
+[[Category: Yu, C]]
-[[Category: Liu, J]]
+[[Category: Cooperativity]]
-[[Category: Hu, X]]
+[[Category: Gene regulation]]
+[[Category: Shelterin]]
+[[Category: Telomere]]