7WME
Crystal Structure of the catalytic domain of At-HIGLE
Summary for 7WME
| Entry DOI | 10.2210/pdb7wme/pdb |
| Descriptor | Structure-specific endonuclease subunit SLX1 homolog, CALCIUM ION (3 entities in total) |
| Functional Keywords | resolvase nuclease structure-selective endonuclease, plant protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 20815.96 |
| Authors | Verma, P.,Kumari, P.,Negi, S.,Yadav, G.,Gaur, V. (deposition date: 2022-01-14, release date: 2022-04-13, Last modification date: 2023-11-29) |
| Primary citation | Verma, P.,Kumari, P.,Negi, S.,Yadav, G.,Gaur, V. Holliday junction resolution by At-HIGLE: an SLX1 lineage endonuclease from Arabidopsis thaliana with a novel in-built regulatory mechanism. Nucleic Acids Res., 50:4630-4646, 2022 Cited by PubMed Abstract: Holliday junction is the key homologous recombination intermediate, resolved by structure-selective endonucleases (SSEs). SLX1 is the most promiscuous SSE of the GIY-YIG nuclease superfamily. In fungi and animals, SLX1 nuclease activity relies on a non-enzymatic partner, SLX4, but no SLX1-SLX4 like complex has ever been characterized in plants. Plants exhibit specialized DNA repair and recombination machinery. Based on sequence similarity with the GIY-YIG nuclease domain of SLX1 proteins from fungi and animals, At-HIGLE was identified to be a possible SLX1 like nuclease from plants. Here, we elucidated the crystal structure of the At-HIGLE nuclease domain from Arabidopsis thaliana, establishing it as a member of the SLX1-lineage of the GIY-YIG superfamily with structural changes in DNA interacting regions. We show that At-HIGLE can process branched-DNA molecules without an SLX4 like protein. Unlike fungal SLX1, At-HIGLE exists as a catalytically active homodimer capable of generating two coordinated nicks during HJ resolution. Truncating the extended C-terminal region of At-HIGLE increases its catalytic activity, changes the nicking pattern, and monomerizes At-HIGLE. Overall, we elucidated the first structure of a plant SLX1-lineage protein, showed its HJ resolving activity independent of any regulatory protein, and identified an in-built novel regulatory mechanism engaging its C-terminal region. PubMed: 35412622DOI: 10.1093/nar/gkac239 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
