3MXN

Crystal structure of the RMI core complex

Summary for 3MXN

• Entry DOI: 10.2210/pdb3mxn/pdb
• Descriptor: RecQ-mediated genome instability protein 1, RecQ-mediated genome instability protein 2, BENZAMIDINE, ... (4 entities in total)
• Functional Keywords: bloom syndrome, helicase, rmi, topoisomerase, replication protein a, replication
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q9H9A7 Q96E14
• Total number of polymer chains: 2
• Total formula weight: 33689.99

Authors

Hoadley, K.A.,Xu, D.,Xue, Y.,Satyshur, K.A.,Wang, W.,Keck, J.L. (deposition date: 2010-05-07, release date: 2010-09-15, Last modification date: 2024-02-21)

Primary citation

Hoadley, K.A.,Xu, D.,Xue, Y.,Satyshur, K.A.,Wang, W.,Keck, J.L.
Structure and cellular roles of the RMI core complex from the bloom syndrome dissolvasome.
Structure, 18:1149-1158, 2010

PubMed Abstract: BLM, the protein product of the gene mutated in Bloom syndrome, is one of five human RecQ helicases. It functions to separate double Holliday junction DNA without genetic exchange as a component of the "dissolvasome," which also includes topoisomerase IIIα and the RMI (RecQ-mediated genome instability) subcomplex (RMI1 and RMI2). We describe the crystal structure of the RMI core complex, comprising RMI2 and the C-terminal OB domain of RMI1. The overall RMI core structure strongly resembles two-thirds of the trimerization core of the eukaryotic single-stranded DNA-binding protein, Replication Protein A. Immunoprecipitation experiments with RMI2 variants confirm key interactions that stabilize the RMI core interface. Disruption of this interface leads to a dramatic increase in cellular sister chromatid exchange events similar to that seen in BLM-deficient cells. The RMI core interface is therefore crucial for BLM dissolvasome assembly and may have additional cellular roles as a docking hub for other proteins.

PubMed: 20826341
DOI: 10.1016/j.str.2010.06.009

Experimental method

X-RAY DIFFRACTION (1.55 Å)