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- EMDB-18946: Cryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51 -

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Entry
Database: EMDB / ID: EMD-18946
TitleCryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51
Map dataAn unsharpened post-processed map of the FIGNL1-RAD51 complex from RELION 4.0
Sample
  • Complex: FIGNL1 hexamer bound to the N-terminus of RAD51
    • Protein or peptide: Fidgetin-like protein 1
    • Protein or peptide: DNA repair protein RAD51 homolog 1
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsAAA / ATPase / DNA repair / HYDROLASE
Function / homology
Function and homology information


microtubule severing ATPase activity / presynaptic intermediate filament cytoskeleton / mitotic recombination-dependent replication fork processing / osteoblast proliferation / chromosome organization involved in meiotic cell cycle / cellular response to camptothecin / telomere maintenance via telomere lengthening / positive regulation of DNA ligation / male meiotic nuclear division / nuclear ubiquitin ligase complex ...microtubule severing ATPase activity / presynaptic intermediate filament cytoskeleton / mitotic recombination-dependent replication fork processing / osteoblast proliferation / chromosome organization involved in meiotic cell cycle / cellular response to camptothecin / telomere maintenance via telomere lengthening / positive regulation of DNA ligation / male meiotic nuclear division / nuclear ubiquitin ligase complex / double-strand break repair involved in meiotic recombination / cellular response to hydroxyurea / DNA recombinase assembly / lateral element / replication-born double-strand break repair via sister chromatid exchange / telomere maintenance via recombination / DNA strand invasion / regulation of DNA damage checkpoint / mitotic recombination / Impaired BRCA2 binding to PALB2 / DNA strand exchange activity / single-stranded DNA helicase activity / reciprocal meiotic recombination / 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 / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / ATP-dependent DNA damage sensor activity / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / regulation of double-strand break repair via homologous recombination / nuclear chromosome / DNA unwinding involved in DNA replication / replication fork processing / Transcriptional Regulation by E2F6 / Presynaptic phase of homologous DNA pairing and strand exchange / ATP-dependent activity, acting on DNA / interstrand cross-link repair / DNA polymerase binding / negative regulation of intrinsic apoptotic signaling pathway / condensed chromosome / ATP metabolic process / condensed nuclear chromosome / male germ cell nucleus / meiotic cell cycle / cellular response to ionizing radiation / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / regulation of protein phosphorylation / double-strand break repair via homologous recombination / HDR through Homologous Recombination (HRR) / PML body / Meiotic recombination / osteoblast differentiation / site of double-strand break / single-stranded DNA binding / double-stranded DNA binding / DNA recombination / chromosome, telomeric region / regulation of cell cycle / hydrolase activity / mitochondrial matrix / DNA repair / centrosome / DNA damage response / chromatin binding / chromatin / nucleolus / negative regulation of apoptotic process / perinuclear region of cytoplasm / enzyme binding / magnesium ion binding / ATP hydrolysis activity / protein-containing complex / mitochondrion / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
: / DNA recombination/repair protein Rad51 / Vps4 oligomerisation, C-terminal / : / Vps4 C terminal oligomerisation domain / 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/repair protein Rad51 / Vps4 oligomerisation, C-terminal / : / Vps4 C terminal oligomerisation domain / 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 / Helix-hairpin-helix domain / 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
DNA repair protein RAD51 homolog 1 / Fidgetin-like protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsCarver A / Yates LA / Zhang X
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Breast Cancer Now United Kingdom
Wellcome Trust United Kingdom
CitationJournal: 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, 2023-
Header (metadata) releaseSep 4, 2024-
Map releaseSep 4, 2024-
UpdateSep 4, 2024-
Current statusSep 4, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18946.png

Downloads & links

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Map

FileDownload / File: emd_18946.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationAn unsharpened post-processed map of the FIGNL1-RAD51 complex from RELION 4.0
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 192 pix.
= 211.2 Å		1.1 Å/pix.
x 192 pix.
= 211.2 Å		1.1 Å/pix.
x 192 pix.
= 211.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.00889
Minimum - Maximum-0.021833094 - 0.057311345
Average (Standard dev.)0.00010495787 (±0.0021694482)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 211.20001 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_18946_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_18946_half_map_1.map
Annotationhalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 1

Fileemd_18946_half_map_2.map
Annotationhalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : FIGNL1 hexamer bound to the N-terminus of RAD51

EntireName: FIGNL1 hexamer bound to the N-terminus of RAD51
Components
  • Complex: FIGNL1 hexamer bound to the N-terminus of RAD51
    • Protein or peptide: Fidgetin-like protein 1
    • Protein or peptide: DNA repair protein RAD51 homolog 1
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: FIGNL1 hexamer bound to the N-terminus of RAD51

SupramoleculeName: FIGNL1 hexamer bound to the N-terminus of RAD51 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 190 KDa

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Macromolecule #1: Fidgetin-like protein 1

MacromoleculeName: Fidgetin-like protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.154504 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAHHHHHHSS GLEVLFQGPK EDSSLPTFKT AKEQLWVDQQ KKYHQPQRAS GSSYGGVKKS LGASRSRGIL GKFVPPIPKQ DGGEQNGGM QCKPYGAGPT EPAHPVDERL KNLEPKMIEL IMNEIMDHGP PVNWEDIAGV EFAKATIKEI VVWPMLRPDI F TGLRGPPK ...String:
MAHHHHHHSS GLEVLFQGPK EDSSLPTFKT AKEQLWVDQQ KKYHQPQRAS GSSYGGVKKS LGASRSRGIL GKFVPPIPKQ DGGEQNGGM QCKPYGAGPT EPAHPVDERL KNLEPKMIEL IMNEIMDHGP PVNWEDIAGV EFAKATIKEI VVWPMLRPDI F TGLRGPPK GILLFGPPGT GKTLIGKCIA SQSGATFFSI SASSLTSKWV GEGEKMVRAL FAVARCQQPA VIFIDQIDSL LS QRGDGEH ESSRRIKTEF LVQLDGATTS SEDRILVVGA TNRPQEIDEA ARRRLVKRLY IPLPEASARK QIVINLMSKE QCC LSEEEI EQIVQQSDAF SGADMTQLCR EASLGPIRSL QTADIATITP DQVRPIAYID FENAFRTVRP SVSPKDLELY ENWN KTFGC GKSAWSHPQF EK

UniProtKB: Fidgetin-like protein 1

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Macromolecule #2: DNA repair protein RAD51 homolog 1

MacromoleculeName: DNA repair protein RAD51 homolog 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.009125 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL INIKGISEAK ADKILAEAAK LVPMGFTTA TEFHQRRSEI IQITTGSKEL DKLLQGGIET GSITEMFGEF RTGKTQICHT LAVTCQLPID RGGGEGKAMY I DTEGTFRP ...String:
MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL INIKGISEAK ADKILAEAAK LVPMGFTTA TEFHQRRSEI IQITTGSKEL DKLLQGGIET GSITEMFGEF RTGKTQICHT LAVTCQLPID RGGGEGKAMY I DTEGTFRP ERLLAVAERY GLSGSDVLDN VAYARAFNTD HQTQLLYQAS AMMVESRYAL LIVDSATALY RTDYSGRGEL SA RQMHLAR FLRMLLRLAD EFGVAVVITN QVVAQVDGAA MFAADPKKPI GGNIIAHAST TRLYLRKGRG ETRICKIYDS PCL PEAEAM FAINADGVGD AKD

UniProtKB: DNA repair protein RAD51 homolog 1

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 6 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 5 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #5: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.5 mg/mL
BufferpH: 8
Component:
ConcentrationFormulaName
100.0 mMNaClSodium chloride
1.0 mMC10H16N5O13P3Adenosine triphosphate
5.0 mMMgCl2Magnesium chloride
1.0 mMC9H15O6PTCEP
20.0 mMC4H11NO3Tris
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 10 sec. / Pretreatment - Atmosphere: AIR / Details: Harrick Plasma Cleaner
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 15406 / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.1 µm / Nominal defocus min: 0.7000000000000001 µm / Nominal magnification: 81000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1800000
Startup modelType of model: INSILICO MODEL / In silico model: Ab-initio in cryoSPARC
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number images used: 57484
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
Final 3D classificationNumber classes: 6 / Avg.num./class: 40000 / Software - Name: RELION (ver. 4.0)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: OTHER
Output model

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

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