4M7C

Crystal structure of the TRF2-binding motif of SLX4 in complex with the TRFH domain of TRF2

Summary for 4M7C

• Entry DOI: 10.2210/pdb4m7c/pdb
• Related: 4M79
• Descriptor: Telomeric repeat-binding factor 2, Peptide from Structure-specific endonuclease subunit SLX4 (3 entities in total)
• Functional Keywords: telomere, t-loop, endonuclease, alt, transcription, endonuclease regulator, dna, hydrolase regulator
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q15554 Q8IY92
• Total number of polymer chains: 4
• Total formula weight: 49842.01

Authors

Wan, B.,Chen, Y.,Wu, J.,Liu, Y.,Lei, M. (deposition date: 2013-08-12, release date: 2013-09-25, Last modification date: 2023-11-08)

Primary citation

Wan, B.,Yin, J.,Horvath, K.,Sarkar, J.,Chen, Y.,Wu, J.,Wan, K.,Lu, J.,Gu, P.,Yu, E.Y.,Lue, N.F.,Chang, S.,Liu, Y.,Lei, M.
SLX4 Assembles a Telomere Maintenance Toolkit by Bridging Multiple Endonucleases with Telomeres
Cell Rep, 4:861-869, 2013

PubMed Abstract: SLX4 interacts with several endonucleases to resolve structural barriers in DNA metabolism. SLX4 also interacts with telomeric protein TRF2 in human cells. The molecular mechanism of these interactions at telomeres remains unknown. Here, we report the crystal structure of the TRF2-binding motif of SLX4 (SLX4TBM) in complex with the TRFH domain of TRF2 (TRF2TRFH) and map the interactions of SLX4 with endonucleases SLX1, XPF, and MUS81. TRF2 recognizes a unique HxLxP motif on SLX4 via the peptide-binding site in its TRFH domain. Telomeric localization of SLX4 and associated nucleases depend on the SLX4-endonuclease and SLX4-TRF2 interactions and the protein levels of SLX4 and TRF2. SLX4 assembles an endonuclease toolkit that negatively regulates telomere length via SLX1-catalyzed nucleolytic resolution of telomere DNA structures. We propose that the SLX4-TRF2 complex serves as a double-layer scaffold bridging multiple endonucleases with telomeres for recombination-based telomere maintenance.

PubMed: 24012755
DOI: 10.1016/j.celrep.2013.08.017

Experimental method

X-RAY DIFFRACTION (2.05 Å)