4XM5

C. glabrata Slx1.

Summary for 4XM5

• Entry DOI: 10.2210/pdb4xm5/pdb
• Descriptor: Structure-specific endonuclease subunit SLX1, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: nuclease, dna repair, giy-yig, homogolous recombination, hydrolase
• Biological source: Candida glabrata (Yeast)
• Cellular location: Nucleus : Q6FML9
• Total number of polymer chains: 1
• Total formula weight: 36647.78

Authors

Gaur, V.,Wyatt, H.D.M.,Komorowska, W.,Szczepanowski, R.H.,de Sanctis, D.,Gorecka, K.M.,West, S.C.,Nowotny, M. (deposition date: 2015-01-14, release date: 2015-03-25, Last modification date: 2024-05-08)

Primary citation

Gaur, V.,Wyatt, H.D.,Komorowska, W.,Szczepanowski, R.H.,de Sanctis, D.,Gorecka, K.M.,West, S.C.,Nowotny, M.
Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease.
Cell Rep, 10:1467-1476, 2015

PubMed Abstract: The SLX1-SLX4 endonuclease required for homologous recombination and DNA repair in eukaryotic cells cleaves a variety of branched DNA structures. The nuclease subunit SLX1 is activated by association with a scaffolding protein SLX4. At the present time, little is known about the structure of SLX1-SLX4 or its mechanism of action. Here, we report the structural insights into SLX1-SLX4 by detailing the crystal structure of Candida glabrata (Cg) Slx1 alone and in combination with the C-terminal region of Slx4. The structure of Slx1 reveals a compact arrangement of the GIY-YIG nuclease and RING domains, which is reinforced by a long α helix. Slx1 forms a stable homodimer that blocks its active site. Slx1-Slx4 interaction is mutually exclusive with Slx1 homodimerization, suggesting a mechanism for Slx1 activation by Slx4.

PubMed: 25753413
DOI: 10.1016/j.celrep.2015.02.019

Experimental method

X-RAY DIFFRACTION (2.34 Å)