3NBH

Crystal structure of human RMI1C-RMI2 complex

Summary for 3NBH

• Entry DOI: 10.2210/pdb3nbh/pdb
• Related: 3NBI
• Descriptor: RecQ-mediated genome instability protein 1, RecQ-mediated genome instability protein 2 (3 entities in total)
• Functional Keywords: two ob-folds containing complex, rpa-like complex, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q9H9A7 Q96E14
• Total number of polymer chains: 2
• Total formula weight: 33616.99

Authors

Wang, F.,Yang, Y.,Singh, T.R.,Busygina, V.,Guo, R.,Wan, K.,Wang, W.,Sung, P.,Meetei, A.R.,Lei, M. (deposition date: 2010-06-03, release date: 2010-09-22, Last modification date: 2024-10-30)

Primary citation

Wang, F.,Yang, Y.,Singh, T.R.,Busygina, V.,Guo, R.,Wan, K.,Wang, W.,Sung, P.,Meetei, A.R.,Lei, M.
Crystal Structures of RMI1 and RMI2, Two OB-Fold Regulatory Subunits of the BLM Complex.
Structure, 18:1159-1170, 2010

PubMed Abstract: Mutations in BLM, a RecQ-like helicase, are linked to the autosomal recessive cancer-prone disorder Bloom's syndrome. BLM associates with topoisomerase (Topo) IIIα, RMI1, and RMI2 to form the BLM complex that is essential for genome stability. The RMI1-RMI2 heterodimer stimulates the dissolution of double Holliday junction into non-crossover recombinants mediated by BLM-Topo IIIα and is essential for stabilizing the BLM complex. However, the molecular basis of these functions of RMI1 and RMI2 remains unclear. Here we report the crystal structures of multiple domains of RMI1-RMI2, providing direct confirmation of the existence of three oligonucleotide/oligosaccharide binding (OB)-folds in RMI1-RMI2. Our structural and biochemical analyses revealed an unexpected insertion motif in RMI1N-OB, which is important for stimulating the dHJ dissolution. We also revealed the structural basis of the interaction between RMI1C-OB and RMI2-OB and demonstrated the functional importance of the RMI1-RMI2 interaction in genome stability maintenance.

PubMed: 20826342
DOI: 10.1016/j.str.2010.06.008

Experimental method

X-RAY DIFFRACTION (2 Å)