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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | BCL7A and BAF47 in a nucleosome bound state | ||||||||||||
Map data | |||||||||||||
Sample |
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Keywords | Nucleosome / acidic patch / BCL7A / arginine anchor / STRUCTURAL PROTEIN | ||||||||||||
| Biological species | Homo sapiens (human) / | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.34 Å | ||||||||||||
Authors | Martin F / Bergamin E | ||||||||||||
| Funding support | France, 3 items
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Citation | Journal: Nucleic Acids Res / Year: 2025Title: Structure of the nucleosome-bound human BCL7A. Authors: Franck Martin / Asgar Abbas Kazrani / Julie Lafouge / Dana Mariel Diaz-Jimenez / Stéphanie Siebert / Leonie Fabbro-Burtschell / Emma Maillard / Karine Lapouge / Haydyn David Thomas Mertens ...Authors: Franck Martin / Asgar Abbas Kazrani / Julie Lafouge / Dana Mariel Diaz-Jimenez / Stéphanie Siebert / Leonie Fabbro-Burtschell / Emma Maillard / Karine Lapouge / Haydyn David Thomas Mertens / Claude Sauter / Alexander Leitner / Françoise Ochsenbein / Alexandre Blais / Elisa Bergamin / ![]() Abstract: Proteins of the BCL7 family (BCL7A, BCL7B, and BCL7C) are among the most recently identified subunits of the mammalian SWI/SNF chromatin remodeler complex and are absent from the unicellular version ...Proteins of the BCL7 family (BCL7A, BCL7B, and BCL7C) are among the most recently identified subunits of the mammalian SWI/SNF chromatin remodeler complex and are absent from the unicellular version of this complex. Their function in the complex is unknown, and very limited structural information is available, despite the fact that they are mutated in several cancer types, most notably blood malignancies and hence medically relevant. Here, using cryo-electron microscopy in combination with biophysical and biochemical approaches, we show that BCL7A forms a stable, high-affinity complex with the nucleosome core particle (NCP) through binding of BCL7A with the acidic patch of the nucleosome via an arginine anchor motif. This interaction is impaired by BCL7A mutations found in cancer. Further, we determined that BCL7A contributes to the remodeling activity of the mSWI/SNF complex and we examined its function at the genomic level. Our findings reveal how BCL7 proteins interact with the NCP and help rationalize the impact of cancer-associated mutations. By providing structural information on the positioning of BCL7 on the NCP, our results broaden the understanding of the mechanism by which SWI/SNF recognizes the chromatin fiber. | ||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51375.map.gz | 68.2 MB | EMDB map data format | |
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| Header (meta data) | emd-51375-v30.xml emd-51375.xml | 18 KB 18 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51375_fsc.xml | 10.9 KB | Display | FSC data file |
| Images | emd_51375.png | 52.5 KB | ||
| Masks | emd_51375_msk_1.map | 137.1 MB | Mask map | |
| Filedesc metadata | emd-51375.cif.gz | 5.4 KB | ||
| Others | emd_51375_half_map_1.map.gz emd_51375_half_map_2.map.gz | 127.2 MB 127.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51375 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51375 | HTTPS FTP |
-Validation report
| Summary document | emd_51375_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_51375_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_51375_validation.xml.gz | 19.7 KB | Display | |
| Data in CIF | emd_51375_validation.cif.gz | 25.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51375 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51375 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_51375.map.gz / Format: CCP4 / Size: 137.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.901 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51375_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_51375_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_51375_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : nucleosome-bound human BCL7A
| Entire | Name: nucleosome-bound human BCL7A |
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| Components |
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-Supramolecule #1: nucleosome-bound human BCL7A
| Supramolecule | Name: nucleosome-bound human BCL7A / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2, #4, #3, #5-#6 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Histone H3.2
| Macromolecule | Name: Histone H3.2 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: |
| Recombinant expression | Organism: ![]() |
| Sequence | String: ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAVM ALQEASEAYL VALFEDTNLC AIHAKRVTIM PKDIQLARRI RGERA |
-Macromolecule #2: Histone H4
| Macromolecule | Name: Histone H4 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: |
| Recombinant expression | Organism: ![]() |
| Sequence | String: SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYAL KRQGRTLYGF GG |
-Macromolecule #3: Histone H2A
| Macromolecule | Name: Histone H2A / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: |
| Recombinant expression | Organism: ![]() |
| Sequence | String: SGRGKQGGKT RAKAKTRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAVRND EELNKLLGRV TIAQGGVLPN IQSVLLPKK |
-Macromolecule #4: Histone H2B
| Macromolecule | Name: Histone H2B / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: |
| Recombinant expression | Organism: ![]() |
| Sequence | String: PEPAKSAPAP KKGSKKAVTK TQKKDGKKRR KTRKESYAIY VYKVLKQVHP DTGISSKAMS IMNSFVNDVF ERIAGEASRL AHYNKRSTIT SREIQTAVRL LLPGELAKHA VSEGTKAVTK YTSAK |
-Macromolecule #5: BAF47
| Macromolecule | Name: BAF47 / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER KKIVASSHG KKTKPNTKDH GYTTLATSVT LLKASEVEEI LDGNDEKYKA VSISTEPPTY L REQKAKRN SQWVPTLPNS SHHLDAVPCS TTINRNRMGR DKKRTFPLCF ...String: MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER KKIVASSHG KKTKPNTKDH GYTTLATSVT LLKASEVEEI LDGNDEKYKA VSISTEPPTY L REQKAKRN SQWVPTLPNS SHHLDAVPCS TTINRNRMGR DKKRTFPLCF DDHDPAVIHE NA SQPEVLV PIRLDMEIDG QKLRDAFTWN MNEKLMTPEM FSEILCDDLD LNPLTFVPAI ASA IRQQIE SYPTDSILED QSDQRVIIKL NIHVGNISLV DQFEWDMSEK ENSPEKFALK LCSE LGLGG EFVTTIAYSI RGQLSWHQKT YAFSENPLPT VEIAIRNTGD ADQWCPLLET LTDAE MEKK IRDQDRNTRR MRRLANTAPA W |
-Macromolecule #6: BCL7A
| Macromolecule | Name: BCL7A / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSGRSVRAET RSRAKDDIKR VMAAIEKVRK WEKKWVTVGD TSLRIYKWVP VTEPKVDDKN KNKKKGKDE KCGSEVTTPE NSSSPGMMDM HDDNSNQSSI ADASPIKQEN SSNSSPAPEP N SAVPSDGT EAKVDEAQAD GKEHPGAEDA SDEQNSQSSM EHSMNSSEKV ...String: MSGRSVRAET RSRAKDDIKR VMAAIEKVRK WEKKWVTVGD TSLRIYKWVP VTEPKVDDKN KNKKKGKDE KCGSEVTTPE NSSSPGMMDM HDDNSNQSSI ADASPIKQEN SSNSSPAPEP N SAVPSDGT EAKVDEAQAD GKEHPGAEDA SDEQNSQSSM EHSMNSSEKV DRQPSGDSGL AA ETSAISQ VPRSRSQRGS QIGREPIGLS GDLEGVPPSK KMKLEASQQN SEEM |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.93 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
France, 3 items
Citation




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Y (Row.)
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Processing
FIELD EMISSION GUN


