5xxf

From Proteopedia

(Difference between revisions)

Revision as of 06:21, 20 December 2017

Crystal structure of Poz1, Tpz1 and Rap1

Structural highlights

5xxf is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5xxe
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POZ1_SCHPO] Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.^[1] [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.^[2] ^[3]

Publication Abstract from PubMed

Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.

Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.,Xue J, Chen H, Wu J, Takeuchi M, Inoue H, Liu Y, Sun H, Chen Y, Kanoh J, Lei M Cell Res. 2017 Dec;27(12):1503-1520. doi: 10.1038/cr.2017.145. Epub 2017 Nov 21. PMID:29160296^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Miyoshi T, Kanoh J, Saito M, Ishikawa F. Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length. Science. 2008 Jun 6;320(5881):1341-4. doi: 10.1126/science.1154819. PMID:18535244 doi:http://dx.doi.org/10.1126/science.1154819
↑ Martin-Castellanos C, Blanco M, Rozalen AE, Perez-Hidalgo L, Garcia AI, Conde F, Mata J, Ellermeier C, Davis L, San-Segundo P, Smith GR, Moreno S. A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events. Curr Biol. 2005 Nov 22;15(22):2056-62. PMID:16303567 doi:http://dx.doi.org/S0960-9822(05)01277-7
↑ Miyoshi T, Kanoh J, Saito M, Ishikawa F. Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length. Science. 2008 Jun 6;320(5881):1341-4. doi: 10.1126/science.1154819. PMID:18535244 doi:http://dx.doi.org/10.1126/science.1154819
↑ Xue J, Chen H, Wu J, Takeuchi M, Inoue H, Liu Y, Sun H, Chen Y, Kanoh J, Lei M. Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex. Cell Res. 2017 Dec;27(12):1503-1520. doi: 10.1038/cr.2017.145. Epub 2017 Nov 21. PMID:29160296 doi:http://dx.doi.org/10.1038/cr.2017.145

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xxf"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5xxf is ON HOLD  until Paper Publication
+==Crystal structure of Poz1, Tpz1 and Rap1==
+<StructureSection load='5xxf' size='340' side='right' caption='[[5xxf]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5xxf]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XXF 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xxe|5xxe]]</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=5xxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xxf OCA], [http://pdbe.org/5xxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xxf RCSB], [http://www.ebi.ac.uk/pdbsum/5xxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xxf 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/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 ==
+Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.
-Authors: Xue, J., Chen, H., Wu, J., Lei, M.
+Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.,Xue J, Chen H, Wu J, Takeuchi M, Inoue H, Liu Y, Sun H, Chen Y, Kanoh J, Lei M Cell Res. 2017 Dec;27(12):1503-1520. doi: 10.1038/cr.2017.145. Epub 2017 Nov 21. PMID:29160296<ref>PMID:29160296</ref>
-Description: Crystal structure of Poz1, Tpz1 and Rap1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Lei, M]]
+<div class="pdbe-citations 5xxf" style="background-color:#fffaf0;"></div>
-[[Category: Xue, J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Chen, H]]
+[[Category: Lei, M]]
 [[Category: Wu, J]]
+[[Category: Xue, J]]
+[[Category: Dna binding protein]]
+[[Category: Hub]]
+[[Category: Sheterin]]
+[[Category: Telomere]]

5xxf

From Proteopedia

Revision as of 06:21, 20 December 2017

Crystal structure of Poz1, Tpz1 and Rap1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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