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- PDB-8r64: Cryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51 -

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Entry
Database: PDB / ID: 8r64
TitleCryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51
Components
  • DNA repair protein RAD51 homolog 1
  • Fidgetin-like protein 1
KeywordsHYDROLASE / AAA / ATPase / DNA repair
Function / homology
Function and homology information


osteoblast proliferation / microtubule severing ATPase activity / microtubule severing / presynaptic intermediate filament cytoskeleton / response to glucoside / male meiotic nuclear division / mitotic recombination-dependent replication fork processing / chromosome organization involved in meiotic cell cycle / cellular response to cisplatin / DNA recombinase assembly ...osteoblast proliferation / microtubule severing ATPase activity / microtubule severing / presynaptic intermediate filament cytoskeleton / response to glucoside / male meiotic nuclear division / mitotic recombination-dependent replication fork processing / chromosome organization involved in meiotic cell cycle / cellular response to cisplatin / DNA recombinase assembly / telomere maintenance via telomere lengthening / double-strand break repair involved in meiotic recombination / cellular response to camptothecin / homologous recombination / DNA strand invasion / mitotic recombination / lateral element / DNA strand exchange activity / Impaired BRCA2 binding to PALB2 / telomere maintenance via recombination / regulation of DNA damage checkpoint / reciprocal meiotic recombination / single-stranded DNA helicase activity / regulation of double-strand break repair via homologous recombination / HDR through Single Strand Annealing (SSA) / ATP-dependent DNA damage sensor activity / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / nuclear chromosome / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / Transcriptional Regulation by E2F6 / Impaired BRCA2 binding to RAD51 / replication fork processing / response to X-ray / Presynaptic phase of homologous DNA pairing and strand exchange / ATP-dependent activity, acting on DNA / interstrand cross-link repair / ATP metabolic process / condensed chromosome / DNA polymerase binding / cellular response to ionizing radiation / condensed nuclear chromosome / cellular response to gamma radiation / meiotic cell cycle / protein-DNA complex / PML body / double-strand break repair via homologous recombination / Meiotic recombination / response to toxic substance / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / HDR through Homologous Recombination (HRR) / osteoblast differentiation / single-stranded DNA binding / site of double-strand break / double-stranded DNA binding / DNA recombination / chromosome, telomeric region / regulation of cell cycle / response to xenobiotic stimulus / mitochondrial matrix / hydrolase activity / DNA repair / centrosome / chromatin binding / DNA damage response / nucleolus / negative regulation of apoptotic process / chromatin / perinuclear region of cytoplasm / magnesium ion binding / enzyme binding / ATP hydrolysis activity / protein-containing complex / mitochondrion / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
: / Vps4 oligomerisation, C-terminal / : / Vps4 C terminal oligomerisation domain / DNA recombination/repair protein Rad51 / DNA recombination and repair protein, RecA-like / DNA recombination and repair protein Rad51-like, C-terminal / Rad51 / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 2. ...: / Vps4 oligomerisation, C-terminal / : / Vps4 C terminal oligomerisation domain / DNA recombination/repair protein Rad51 / DNA recombination and repair protein, RecA-like / DNA recombination and repair protein Rad51-like, C-terminal / Rad51 / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 2. / DNA recombination and repair protein RecA-like, ATP-binding domain / RecA family profile 1. / : / DNA repair Rad51/transcription factor NusA, alpha-helical / SAM-like Helix-hairpin-helix tandem / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / DNA repair protein RAD51 homolog 1 / Fidgetin-like protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsCarver, A. / Yates, L.A. / Zhang, X.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Breast Cancer Now United Kingdom
Wellcome Trust United Kingdom
Citation
Journal: Science / Year: 2025
Title: Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.
Authors: Alexander Carver / Tai-Yuan Yu / Luke A Yates / Travis White / Raymond Wang / Katie Lister / Maria Jasin / Xiaodong Zhang /
Abstract: Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central component of several crucial processes in repairing DNA and protecting genome integrity, forms ...Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central component of several crucial processes in repairing DNA and protecting genome integrity, forms filaments on DNA, which are tightly regulated. One of these RAD51 regulators is FIGNL1 (fidgetin-like 1), which prevents RAD51 genotoxic chromatin association in normal cells and persistent RAD51 foci upon DNA damage. The cryogenic electron microscopy-imaged structure of FIGNL1 in complex with RAD51 reveals that FIGNL1 forms a nonplanar hexamer and encloses RAD51 N terminus in the FIGNL1 hexamer pore. Mutations in pore loop or catalytic residues of FIGNL1 render it defective in filament disassembly and are lethal in mouse embryonic stem cells. Our study reveals a distinct mechanism for removing RAD51 from bound substrates and provides the molecular basis for FIGNL1 in maintaining genome stability.
#1: Journal: bioRxiv / Year: 2024
Title: Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.
Authors: Alexander Carver / Tai-Yuan Yu / Luke A Yates / Travis White / Raymond Wang / Katie Lister / Maria Jasin / Xiaodong Zhang /
Abstract: Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central player of several crucial processes in repairing and protecting genome integrity, forms filaments ...Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central player of several crucial processes in repairing and protecting genome integrity, forms filaments on DNA. RAD51 filaments are tightly regulated. One of these regulators is FIGNL1, that prevents persistent RAD51 foci post-damage and genotoxic chromatin association in cells. The cryogenic electron microscopy structure of FIGNL1 in complex with RAD51 reveals that the FIGNL1 forms a non-planar hexamer and RAD51 N-terminus is enclosed in the FIGNL1 hexamer pore. Mutations in pore loop or catalytic residues of FIGNL1 render it defective in filament disassembly and are lethal in mouse embryonic stem cells. Our study reveals a unique mechanism for removing RAD51 from DNA and provides the molecular basis for FIGNL1 in maintaining genome stability.
History
DepositionNov 20, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 4, 2024Provider: repository / Type: Initial release
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Revision 1.1Jan 8, 2025Group: Data collection / Database references / Structure summary
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Fidgetin-like protein 1
C: Fidgetin-like protein 1
D: Fidgetin-like protein 1
E: Fidgetin-like protein 1
F: Fidgetin-like protein 1
A: Fidgetin-like protein 1
G: DNA repair protein RAD51 homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)317,04519
Polymers313,9367
Non-polymers3,10912
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Fidgetin-like protein 1


Mass: 46154.504 Da / Num. of mol.: 6 / Mutation: E501Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FIGNL1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6PIW4
#2: Protein DNA repair protein RAD51 homolog 1 / HsRAD51 / hRAD51 / RAD51 homolog A


Mass: 37009.125 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAD51, RAD51A, RECA / Production host: Escherichia coli (E. coli) / References: UniProt: Q06609
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP, energy-carrying molecule*YM
#5: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: FIGNL1 hexamer bound to the N-terminus of RAD51 / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightValue: 0.19 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
Buffer component
IDConc.NameFormulaBuffer-ID
1100 mMSodium chlorideNaCl1
21 mMAdenosine triphosphateC10H16N5O13P31
35 mMMagnesium chlorideMgCl21
41 mMTCEPC9H15O6P1
520 mMTrisC4H11NO31
SpecimenConc.: 0.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: Harrick Plasma Cleaner / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2100 nm / Nominal defocus min: 700 nm / Cs: 2.7 mm
Specimen holderSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 15406

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.1.2particle selection
2RELION4particle selection
3EPUimage acquisition
5CTFFIND4.1CTF correction
8PHENIXmodel fitting
9Cootmodel fitting
11RELION4initial Euler assignment
12RELION4final Euler assignment
13RELION4classification
14RELION43D reconstruction
15PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1800000
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 57484 / Symmetry type: POINT
Atomic model buildingProtocol: OTHER / Space: REAL
Atomic model buildingSource name: AlphaFold / Type: in silico model
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00213869
ELECTRON MICROSCOPYf_angle_d0.5518842
ELECTRON MICROSCOPYf_dihedral_angle_d10.8621964
ELECTRON MICROSCOPYf_chiral_restr0.042181
ELECTRON MICROSCOPYf_plane_restr0.0032414

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