Fig. 4: Structure of the full MEILB2–BRME1MBD 2:2 complex.
From: MEILB2-BRME1 forms a V-shaped DNA clamp upon BRCA2-binding in meiotic recombination
a AlphaFold2 model of the full MEILB2–BRME1MBD 2:2 complex, generated using the MEILB2α–BRME1MBD 2:2 structure reported herein (PDB accession 7Z8Z), and the MEILB2 ARM domain structure (PDB accession 7LDG)43, as the sole templates. The molecule has a length of ~18 nm, including a 14-nm separation between the N-terminal four-helical bundle and the C-terminal ARM domains. Modelling details, scores and plots are provided in Supplementary Fig. 5. b SEC-SAXS scattering curves of the MEILB2–BRME1MBD full complex and the MEILB2α–BRME1MBD core complex, overlaid with the theoretical scattering curves of the AlphaFold2 model (blue), a deformed and shortened version of the AlphaFold2 model (red; Supplementary Fig. 6d), and the core crystal structure (yellow), with χ2 values of 2.96, 21.08 and 2.50, respectively. Residuals for each fit are shown (inset). Guinier analyses and real-space P(r) distributions are shown in Supplementary Fig. 6. c Schematic of the MEILB2–BRME1MBD 2:2 structure.
