4ZDT

Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4

Summary for 4ZDT

• Entry DOI: 10.2210/pdb4zdt/pdb
• Descriptor: Structure-specific endonuclease subunit slx1, Structure-specific endonuclease subunit slx4, ZINC ION, ... (6 entities in total)
• Functional Keywords: ring finger, endonuclease, hydrolase
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); More
• Cellular location: Nucleus, nucleolus : Q9P7M3 Q9P6M0
• Total number of polymer chains: 4
• Total formula weight: 34189.03

Authors

Lian, F.M.,Xie, S.,Qian, C.M. (deposition date: 2015-04-19, release date: 2016-02-03, Last modification date: 2024-03-20)

Primary citation

Lian, F.M.,Xie, S.,Qian, C.M.
Crystal structure and SUMO binding of Slx1-Slx4 complex
Sci Rep, 6:19331-19331, 2016

PubMed Abstract: The SLX1-SLX4 complex is a structure-specific endonuclease that cleaves branched DNA structures and plays significant roles in DNA recombination and repair in eukaryotic cells. The heterodimeric interaction between SLX1 and SLX4 is essential for the endonuclease activity of SLX1. Here, we present the crystal structure of Slx1 C-terminal zinc finger domain in complex with the C-terminal helix-turn-helix domain of Slx4 from Schizosaccharomyces pombe at 2.0 Å resolution. The structure reveals a conserved binding mechanism underling the Slx1-Slx4 interaction. Structural and sequence analyses indicate Slx1 C-terminal domain is actually an atypical C4HC3-type RING finger which normally possesses E3 ubiquitin ligase activity, but here is absolutely required for Slx1 interaction with Slx4. Furthermore, we found the C-terminal tail of S. pombe Slx1 contains a SUMO-interacting motif and can recognize Pmt3 (S. pombe SUMO), suggesting that Slx1-Slx4 complex could be recruited by SUMOylated protein targets to take part in replication associated DNA repair processes.

PubMed: 26787556
DOI: 10.1038/srep19331

Experimental method

X-RAY DIFFRACTION (2 Å)