6J8Y

Crystal structure of the human RAD9-HUS1-RAD1-RHINO complex

Summary for 6J8Y

• Entry DOI: 10.2210/pdb6j8y/pdb
• Descriptor: Cell cycle checkpoint control protein RAD9A, Checkpoint protein HUS1, Cell cycle checkpoint protein RAD1, ... (5 entities in total)
• Functional Keywords: dna damage, checkpoint, dna repair, dna binding clamp, cell cycle, exonuclease, hydrolase, nuclease, nucleus, phosphoprotein, pcna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 96367.69

Authors

Hara, K.,Iida, N.,Sakurai, H.,Hashimoto, H. (deposition date: 2019-01-21, release date: 2019-12-04, Last modification date: 2024-11-06)

Primary citation

Hara, K.,Iida, N.,Tamafune, R.,Ohashi, E.,Sakurai, H.,Ishikawa, Y.,Hishiki, A.,Hashimoto, H.
Structure of the RAD9-RAD1-HUS1 checkpoint clamp bound to RHINO sheds light on the other side of the DNA clamp.
J.Biol.Chem., 295:899-904, 2020

PubMed Abstract: DNA clamp, a highly conserved ring-shaped protein, binds dsDNA within its central pore. Also, DNA clamp interacts with various nuclear proteins on its front, thereby stimulating their enzymatic activities and biological functions. It has been assumed that the DNA clamp is a functionally single-faced ring from bacteria to humans. Here, we report the crystal structure of the heterotrimeric RAD9-RAD1-HUS1 (9-1-1) checkpoint clamp bound to a peptide of RHINO, a recently identified cancer-related protein that interacts with 9-1-1 and promotes activation of the DNA damage checkpoint. This is the first structure of 9-1-1 bound to its partner. The structure reveals that RHINO is unexpectedly bound to the edge and around the back of the 9-1-1 ring through specific interactions with the RAD1 subunit of 9-1-1. Our finding indicates that 9-1-1 is a functionally double-faced DNA clamp.

PubMed: 31776186
DOI: 10.1074/jbc.AC119.011816

Experimental method

X-RAY DIFFRACTION (2.4 Å)