View source for 8ynu


==Crystal structure of the myb domain of S.pombe Tbf1 in the P222 space group==
<StructureSection load='8ynu' size='340' side='right'caption='[[8ynu]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ynu]] is a 2 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=8YNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YNU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8ynu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ynu OCA], [https://pdbe.org/8ynu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ynu RCSB], [https://www.ebi.ac.uk/pdbsum/8ynu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ynu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRF1_SCHPO TRF1_SCHPO] Binds the telomeric double-stranded TTACAGG repeat and regulates telomere length.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Telomeric repeat-binding factor 1 (Tbf1) has a similar architecture as the TRF family of telomeric proteins and plays important roles in both telomere homeostasis and ribosome regulation. However, the molecular basis of why Tbf1 has such different functions compared to other TRFs remains unclear. Here, we present the crystal structures of the TRF homology (TRFH) and Myb-L domains from Schizosaccharomyces pombe Tbf1 (spTbf1). TRFH-mediated homodimerization is essential for spTbf1 stability. Importantly, spTbf1(TRFH) lacks the conserved docking motif for interactions with telomeric proteins, explaining why spTbf1 does not participate in the assembly of the shelterin complex. Finally, structural and biochemical analyses demonstrate that TRFH and Myb-L domains as well as the loop region of spTbf1 coordinate to recognize S. pombe telomeric double-stranded DNA. Overall, our findings provide structural and functional insights into how fungi Tbf1 acts as an atypical telomeric repeat-binding factor, which helps to understand the evolution of TRFH-containing telomeric proteins.

Structural and functional insights into yeast Tbf1 as an atypical telomeric repeat-binding factor.,Wu Z, Gu X, Zha L, Yang Q, Zhou Y, Zeng Z Structure. 2024 Jul 11;32(7):889-898.e3. doi: 10.1016/j.str.2024.04.002. Epub , 2024 Apr 26. PMID:38677290<ref>PMID:38677290</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ynu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Wu ZF]]
[[Category: Zhou YZ]]