Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures and molecular mechanisms of RAD54B in modulating homologous recombination.
Journal, issue, pages	bioRxiv, Year 2026
Publish date	Mar 24, 2026
Authors	Pengtao Liang / Stephanie Tye / Johanna Ertl da Costa / Neelam Maharshi / Bilge Argunhan / Lucas Kuhlen / Megan Battley / Elizabeth A McCormack / Wolf-Dietrich Heyer / Markus Löbrich / Xiaodong Zhang /
PubMed Abstract	Genome stability is essential for cellular viability yet constantly threatened by endogenous and exogenous DNA-damaging agents. Among these, DNA double-strand breaks (DSBs) are particularly harmful ...Genome stability is essential for cellular viability yet constantly threatened by endogenous and exogenous DNA-damaging agents. Among these, DNA double-strand breaks (DSBs) are particularly harmful and in S/G2 phases are faithfully repaired through homologous recombination (HR), a high-fidelity pathway utilising homologous sequences in sister chromatin. The RAD51 recombinase forms nucleoprotein filaments on single-stranded DNA (ssDNA) to mediate homology search, strand invasion and subsequent D-loop formation that leads to DNA synthesis and repair. The efficiency of HR depends on precise regulation of RAD51 filament dynamics by accessory factors, including RAD54 and RAD54B, which belong to the SWI2/SNF2-family DNA translocases. While RAD54 is well-characterized, RAD54B's molecular functions remain poorly understood. Here, we define RAD54B's role in HR using cryo-electron microscopy, mutagenesis, biochemical and cellular assays. We show that RAD54B stabilizes RAD51-DNA filaments, inhibits RAD51 ATPase activity, and promotes strand invasion, D-loop formation and strand exchange. The N-terminal domain (NTD) alone supports filament stabilization and strand exchange, while the C-terminal ATPase domain is required for D-loop formation. Structural and biochemical analyses reveal three RAD51-interacting sites within the NTD and a unique domain (β-domain) that bridges RAD51 protomers and contacts donor dsDNA. This β-domain also regulates RAD54B's ATPase activity and higher-order oligomer organization on dsDNA. Cellular assays reveal that the NTD RAD51-interacting sites as well as the β-domain are required for repairing camptothecin-induced DSBs by HR in human cells. Our findings uncover a modular architecture and mechanistic framework for RAD54B function in HR, highlighting its critical role in genome maintenance.
External links	bioRxiv / PubMed:41929041 / PubMed Central
Methods	EM (single particle)
Resolution	2.4 - 3.2 Å
Structure data	55166 9srz EMDB-55166, PDB-9srz: RAD51-ssDNA filament in complex with calcium and ATP bound by the RAD54B N-terminus Method: EM (single particle) / Resolution: 2.61 Å 55189 9ssl EMDB-55189, PDB-9ssl: RAD51-ssDNA filament in complex with magnesium and ATP bound by the RAD54B N-terminus (peptide) Method: EM (single particle) / Resolution: 2.9 Å 56178 9trl EMDB-56178, PDB-9trl: RAD51-ssDNA filament in complex with magnesium and ATP bound by the RAD54B N-terminus (beta-barrel) Method: EM (single particle) / Resolution: 3.0 Å 56179 9trm EMDB-56179, PDB-9trm: RAD51-dsDNA filament in complex with calcium and ATP bound by the RAD54B N-terminus Method: EM (single particle) / Resolution: 2.4 Å 56447 9tyy EMDB-56447, PDB-9tyy: RAD51-ssDNA filament in complex with calcium and ATP bound by the RAD54 N-terminus Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-CA: Unknown entry ChemComp-K: Unknown entry ChemComp-MG*: Unknown entry
Source	homo sapiens (human) synthetic construct (others) homo (humans)
Keywords	DNA BINDING PROTEIN / RAD51 recombinase / RAD54B / filament modulation / homologous recombination / RAD54