8ynu | pdb_00008ynu

Crystal structure of the myb domain of S.pombe Tbf1 in the P222 space group

spinqualitylabelsall models 8ynu, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ynu is a 2 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.76Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRF1_SCHPO Binds the telomeric double-stranded TTACAGG repeat and regulates telomere length. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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