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Open data
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Basic information
Entry | Database: PDB / ID: 9f5w | |||||||||||||||||||||
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Title | Human condensin II - M18BP1 complex | |||||||||||||||||||||
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![]() | DNA BINDING PROTEIN / Chromosome organisation complex | |||||||||||||||||||||
Function / homology | ![]() female meiosis chromosome separation / positive regulation of chromosome condensation / histone H4K20me1 reader activity / positive regulation of chromosome separation / meiotic chromosome condensation / positive regulation of chromosome segregation / condensin complex / kinetochore organization / bHLH transcription factor binding / meiotic chromosome segregation ...female meiosis chromosome separation / positive regulation of chromosome condensation / histone H4K20me1 reader activity / positive regulation of chromosome separation / meiotic chromosome condensation / positive regulation of chromosome segregation / condensin complex / kinetochore organization / bHLH transcription factor binding / meiotic chromosome segregation / mitotic sister chromatid separation / condensed chromosome, centromeric region / mitotic chromosome condensation / Condensation of Prometaphase Chromosomes / chromosome condensation / inner cell mass cell proliferation / nuclear chromosome / detection of maltose stimulus / maltose transport complex / carbohydrate transport / pericentric heterochromatin / mitotic sister chromatid segregation / chromosome, centromeric region / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / intercellular bridge / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / condensed chromosome / Deposition of new CENPA-containing nucleosomes at the centromere / ATP-binding cassette (ABC) transporter complex / Condensation of Prophase Chromosomes / condensed nuclear chromosome / erythrocyte differentiation / cell chemotaxis / cell junction / T cell differentiation in thymus / single-stranded DNA binding / outer membrane-bounded periplasmic space / histone binding / transcription by RNA polymerase II / periplasmic space / nuclear speck / cell division / DNA damage response / chromatin binding / chromatin / nucleolus / ATP hydrolysis activity / DNA binding / extracellular exosome / nucleoplasm / ATP binding / nucleus / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() ![]() ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.5 Å | |||||||||||||||||||||
![]() | Borsellini, A. / Vannini, A. | |||||||||||||||||||||
Funding support | European Union, 1items
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![]() | ![]() Title: Condensin II activation by M18BP1. Authors: Alessandro Borsellini / Duccio Conti / Erin E Cutts / Rebecca J Harris / Kai Walstein / Andrea Graziadei / Valentina Cecatiello / Tom F Aarts / Ren Xie / Abdelghani Mazouzi / Sushweta Sen / ...Authors: Alessandro Borsellini / Duccio Conti / Erin E Cutts / Rebecca J Harris / Kai Walstein / Andrea Graziadei / Valentina Cecatiello / Tom F Aarts / Ren Xie / Abdelghani Mazouzi / Sushweta Sen / Claire Hoencamp / Richard Pleuger / Sabrina Ghetti / Lina Oberste-Lehn / Dongqing Pan / Tanja Bange / Judith H I Haarhuis / Anastassis Perrakis / Thijn R Brummelkamp / Benjamin D Rowland / Andrea Musacchio / Alessandro Vannini / ![]() ![]() ![]() ![]() Abstract: Condensin I and II promote the drastic spatial rearrangement of the human genome upon mitotic entry. While condensin II is known to initiate this process in early mitosis, what triggers its ...Condensin I and II promote the drastic spatial rearrangement of the human genome upon mitotic entry. While condensin II is known to initiate this process in early mitosis, what triggers its activation and loading onto chromatin at this juncture remains unclear. Through genetic and proteomic approaches, we identify MIS18-binding protein 1 (M18BP1), a protein required to maintain centromere identity, as the elusive factor required for condensin II localization to chromatin. M18BP1 directly binds condensin II's CAP-G2 subunit. The condensin II antagonist MCPH1 also binds to CAP-G2 and outcompetes M18BP1 during interphase to maintain the genome in its uncondensed state. A switch from MCPH1 to M18BP1 at mitotic onset activates condensin II, thus promoting proper chromosome condensation. Regulation of this M18BP1-condensin interaction thus determines both the uncondensed state of the interphase genome and its compacted state in mitosis. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 588.9 KB | Display | ![]() |
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PDB format | ![]() | 434.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 74.2 KB | Display | |
Data in CIF | ![]() | 118.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 50201MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Structural maintenance of chromosomes protein ... , 2 types, 2 molecules AB
#1: Protein | Mass: 135872.141 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 149551.078 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Condensin-2 complex subunit ... , 3 types, 3 molecules DHG
#3: Protein | Mass: 169109.938 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#4: Protein | Mass: 72040.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#6: Protein | Mass: 131135.969 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein , 1 types, 1 molecules M
#5: Protein | Mass: 72917.172 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Strain: K12 Gene: malE, b4034, JW3994, MIS18BP1, C14orf106, KIAA1903, KNL2, M18BP1 Production host: ![]() |
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-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Human condensin II holocomplex bound to M18BP1 fragment Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | ||||||||||||||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||
Source (natural) | Organism: ![]() | ||||||||||||||||||||||||
Source (recombinant) | Organism: ![]() | ||||||||||||||||||||||||
Buffer solution | pH: 8.5 | ||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil | ||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 85 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 7.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 24490 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||||||||||
Atomic model building | Source name: AlphaFold / Type: in silico model |