[English] 日本語
Yorodumi- PDB-7q2x: Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7q2x | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I) | ||||||||||||
Components |
| ||||||||||||
Keywords | CELL CYCLE / condensin / SMC | ||||||||||||
Function / homology | Function and homology information negative regulation of meiotic DNA double-strand break formation / Condensation of Prometaphase Chromosomes / meiotic chromosome condensation / tRNA gene clustering / meiotic chromosome separation / condensin complex / DNA secondary structure binding / maintenance of rDNA / rDNA chromatin condensation / synaptonemal complex assembly ...negative regulation of meiotic DNA double-strand break formation / Condensation of Prometaphase Chromosomes / meiotic chromosome condensation / tRNA gene clustering / meiotic chromosome separation / condensin complex / DNA secondary structure binding / maintenance of rDNA / rDNA chromatin condensation / synaptonemal complex assembly / nucleophagy / condensed chromosome, centromeric region / mitotic chromosome condensation / chromosome condensation / silent mating-type cassette heterochromatin formation / minor groove of adenine-thymine-rich DNA binding / mitotic sister chromatid segregation / condensed chromosome / histone binding / double-stranded DNA binding / cell division / chromatin binding / chromatin / nucleolus / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Saccharomyces cerevisiae S288C (yeast) synthetic construct (others) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||||||||
Authors | Lee, B.-G. / Rhodes, J. / Lowe, J. | ||||||||||||
Funding support | United Kingdom, 3items
| ||||||||||||
Citation | Journal: Proc Natl Acad Sci U S A / Year: 2022 Title: Clamping of DNA shuts the condensin neck gate. Authors: Byung-Gil Lee / James Rhodes / Jan Löwe / Abstract: SignificanceDNA needs to be compacted to fit into nuclei and during cell division, when dense chromatids are formed for their mechanical segregation, a process that depends on the protein complex ...SignificanceDNA needs to be compacted to fit into nuclei and during cell division, when dense chromatids are formed for their mechanical segregation, a process that depends on the protein complex condensin. It forms and enlarges loops in DNA through loop extrusion. Our work resolves the atomic structure of a DNA-bound state of condensin in which ATP has not been hydrolyzed. The DNA is clamped within a compartment that has been reported previously in other structural maintenance of chromosomes (SMC) complexes, including Rad50, cohesin, and MukBEF. With the caveat of important differences, it means that all SMC complexes cycle through at least some similar states and undergo similar conformational changes in their head modules, while hydrolyzing ATP and translocating DNA. | ||||||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7q2x.cif.gz | 458.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7q2x.ent.gz | 347.3 KB | Display | PDB format |
PDBx/mmJSON format | 7q2x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7q2x_validation.pdf.gz | 799.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 7q2x_full_validation.pdf.gz | 820.8 KB | Display | |
Data in XML | 7q2x_validation.xml.gz | 51.7 KB | Display | |
Data in CIF | 7q2x_validation.cif.gz | 72.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q2/7q2x ftp://data.pdbj.org/pub/pdb/validation_reports/q2/7q2x | HTTPS FTP |
-Related structure data
Related structure data | 13783MC 7q2yC 7q2zC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
-Structural maintenance of chromosomes protein ... , 2 types, 2 molecules AB
#1: Protein | Mass: 134125.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c / Gene: SMC2, YFR031C / Production host: Saccharomyces cerevisiae (brewer's yeast) / Strain (production host): W303-1a / References: UniProt: P38989 |
---|---|
#2: Protein | Mass: 162435.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: comment: since alignment with full sequence did not work, we input only sequence in pdb. The real sequence is UNIPROT Q12267 (full-length construct),comment: since alignment with full ...Details: comment: since alignment with full sequence did not work, we input only sequence in pdb. The real sequence is UNIPROT Q12267 (full-length construct),comment: since alignment with full sequence did not work, we input only sequence in pdb. The real sequence is UNIPROT Q12267 (full-length construct) Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c / Gene: SMC4, YLR086W, L9449.5 / Production host: Saccharomyces cerevisiae W303 (yeast) / References: UniProt: Q12267 |
-Condensin complex subunit ... , 2 types, 2 molecules CD
#3: Protein | Mass: 86323.297 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c / Gene: BRN1, YBL097W, YBL0830 / Production host: Saccharomyces cerevisiae W303 (yeast) / References: UniProt: P38170 |
---|---|
#4: Protein | Mass: 133116.766 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c / Gene: YCS4, LOC7, YLR272C, L8479.14 / Production host: Saccharomyces cerevisiae W303 (yeast) / References: UniProt: Q06156 |
-DNA chain , 2 types, 2 molecules FG
#5: DNA chain | Mass: 11230.485 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
---|---|
#6: DNA chain | Mass: 10905.983 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 3 types, 6 molecules
#7: Chemical | #8: Chemical | #9: Chemical | |
---|
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3 Type: COMPLEX / Entity ID: #1-#6 / Source: RECOMBINANT |
---|---|
Molecular weight | Value: 515 kDa/nm / Experimental value: YES |
Source (natural) | Organism: Saccharomyces cerevisiae S288C (yeast) |
Source (recombinant) | Organism: Saccharomyces cerevisiae W303 (yeast) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: UltrAuFoil R2/2 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 55 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
EM software |
| ||||||||||||||||||||||||||||||||||||||||
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 286294 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building |
|