7CQ3
Crystal structure of Slx1-Slx4
Summary for 7CQ3
| Entry DOI | 10.2210/pdb7cq3/pdb |
| Related | 7CQ2 |
| Descriptor | Structure-specific endonuclease subunit SLX1, SLX4 isoform 1, ZINC ION, ... (5 entities in total) |
| Functional Keywords | endonuclease complex, holliday junction, slx1-slx4, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 46408.99 |
| Authors | |
| Primary citation | Xu, X.,Wang, M.,Sun, J.,Yu, Z.,Li, G.,Yang, N.,Xu, R.M. Structure specific DNA recognition by the SLX1-SLX4 endonuclease complex. Nucleic Acids Res., 49:7740-7752, 2021 Cited by PubMed Abstract: The SLX1-SLX4 structure-specific endonuclease complex is involved in processing diverse DNA damage intermediates, including resolution of Holliday junctions, collapse of stalled replication forks and removal of DNA flaps. The nuclease subunit SLX1 is inactive on its own, but become activated upon binding to SLX4 via its conserved C-terminal domain (CCD). Yet, how the SLX1-SLX4 complex recognizes specific DNA structure and chooses cleavage sites remains unknown. Here we show, through a combination of structural, biochemical and computational analyses, that the SAP domain of SLX4 is critical for efficient and accurate processing of 5'-flap DNA. It binds the minor groove of DNA about one turn away from the flap junction, and the 5'-flap is implicated in binding the core domain of SLX1. This binding mode accounts for specific recognition of 5'-flap DNA and specification of cleavage site by the SLX1-SLX4 complex. PubMed: 34181713DOI: 10.1093/nar/gkab542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.449 Å) |
Structure validation
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