[English] 日本語
Yorodumi
- EMDB-13786: Cryo-EM structure of S.cerevisiae condensin Ycg1-Brn1-DNA complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-13786
TitleCryo-EM structure of S.cerevisiae condensin Ycg1-Brn1-DNA complex
Map datacropped box=162pix
Sample
  • Complex: complex of condensin ycg1 and DNA
    • Protein or peptide: Condensin complex subunit 3
    • Protein or peptide: Condensin complex subunit 2
    • DNA: DNA
    • DNA: DNA
Function / homology
Function and homology information


negative regulation of meiotic DNA double-strand break formation / meiotic chromosome condensation / Condensation of Prometaphase Chromosomes / tRNA gene clustering / meiotic chromosome separation / condensin complex / rDNA chromatin condensation / synaptonemal complex assembly / mitotic chromosome condensation / chromosome condensation ...negative regulation of meiotic DNA double-strand break formation / meiotic chromosome condensation / Condensation of Prometaphase Chromosomes / tRNA gene clustering / meiotic chromosome separation / condensin complex / rDNA chromatin condensation / synaptonemal complex assembly / mitotic chromosome condensation / chromosome condensation / mitotic sister chromatid segregation / condensed chromosome / cell division / chromatin binding / nucleus / cytoplasm
Similarity search - Function
Nuclear condensin complex subunit 3, C-terminal domain / Condensin complex subunit 3 / Nuclear condensing complex subunits, C-term domain / Condensin complex subunit 2/barren / Condensin complex subunit 2 / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
Condensin complex subunit 2 / Condensin complex subunit 3
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288C (yeast) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsLee B-G / Rhodes J / Lowe J
Funding support United Kingdom, 3 items
OrganizationGrant numberCountry
Wellcome Trust202754/Z/16/Z United Kingdom
Medical Research Council (MRC, United Kingdom)U105184326 United Kingdom
Wellcome Trust218621/Z/19/Z United Kingdom
CitationJournal: 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
DepositionOct 26, 2021-
Header (metadata) releaseApr 6, 2022-
Map releaseApr 6, 2022-
UpdateApr 13, 2022-
Current statusApr 13, 2022Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

emd_13786.png

Downloads & links

-
Map

FileDownload / File: emd_13786.map.gz / Format: CCP4 / Size: 16.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationcropped box=162pix
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.04
Minimum - Maximum-0.11859981 - 0.22150585
Average (Standard dev.)0.00033888465 (±0.010838157)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions162162162
Spacing162162162
CellA=B=C: 174.96 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: cropped box=162pix

Fileemd_13786_half_map_1.map
Annotationcropped box=162pix
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: cropped box=162pix

Fileemd_13786_half_map_2.map
Annotationcropped box=162pix
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : complex of condensin ycg1 and DNA

EntireName: complex of condensin ycg1 and DNA
Components
  • Complex: complex of condensin ycg1 and DNA
    • Protein or peptide: Condensin complex subunit 3
    • Protein or peptide: Condensin complex subunit 2
    • DNA: DNA
    • DNA: DNA

-
Supramolecule #1: complex of condensin ycg1 and DNA

SupramoleculeName: complex of condensin ycg1 and DNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: ycg1-DNA structure from the dataset of complex of condensin pentamer (smc2, smc4, brn1, ycs4, ycg1), DNA, ADP-BeF3
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightExperimental: 120 kDa/nm

-
Macromolecule #1: Condensin complex subunit 3

MacromoleculeName: Condensin complex subunit 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 117.981 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
SequenceString: MQDPDGIDIN TKIFNSVAEV FQKAQGSYAG HRKHIAVLKK IQSKAVEQGY EDAFNFWFDK LVTKILPLKK NEIIGDRIVK LVAAFIASL ERELILAKKQ NYKLTNDEEG IFSRFVDQFI RHVLRGVESP DKNVRFRVLQ LLAVIMDNIG EIDESLFNLL I LSLNKRIY ...String:
MQDPDGIDIN TKIFNSVAEV FQKAQGSYAG HRKHIAVLKK IQSKAVEQGY EDAFNFWFDK LVTKILPLKK NEIIGDRIVK LVAAFIASL ERELILAKKQ NYKLTNDEEG IFSRFVDQFI RHVLRGVESP DKNVRFRVLQ LLAVIMDNIG EIDESLFNLL I LSLNKRIY DREPTVRIQA VFCLTKFQDE EQTEHLTELS DNEENFEATR TLVASIQNDP SAEVRRAAML NLINDNNTRP YI LERARDV NIVNRRLVYS RILKSMGRKC FDDIEPHIFD QLIEWGLEDR ELSVRNACKR LIAHDWLNAL DGDLIELLEK LDV SRSSVC VKAIEALFQS RPDILSKIKF PESIWKDFTV EIAFLFRAIY LYCLDNNITE MLEENFPEAS KLSEHLNHYI LLRY HHNDI SNDSQSHFDY NTLEFIIEQL SIAAERYDYS DEVGRRSMLT VVRNMLALTT LSEPLIKIGI RVMKSLSINE KDFVT MAIE IINDIRDDDI EKQEQEEKIK SKKINRRNET SVDEEDENGT HNDEVNEDEE DDNISSFHSA VENLVQGNGN VSESDI INN LPPEKEASSA TIVLCLTRSS YMLELVNTPL TENILIASLM DTLITPAVRN TAPNIRELGV KNLGLCCLLD VKLAIDN MY ILGMCVSKGN ASLKYIALQV IVDIFSVHGN TVVDGEGKVD SISLHKIFYK VLKNNGLPEC QVIAAEGLCK LFLADVFT D DDLFETLVLS YFSPINSSNE ALVQAFAFCI PVYCFSHPAH QQRMSRTAAD ILLRLCVLWD DLQSSVIPEV DREAMLKPN IIFQQLLFWT DPRNLVNQTG STKKDTVQLT FLIDVLKIYA QIEKKEIKKM IITNINAIFL SSEQDYSTLK ELLEYSDDIA ENDNLDNVS KNALDKLRNN LNSLIEEINE RSETQTKDEN NTANDQYSSI LGNSFNKSSN DTIEHAADIT DGNNTELTKT T VNISAVDN TTEQSNSRKR TRSEAEQIDT SKNLENMSIQ DTSTVAKNVS FVLPDEKSDA MSIDEEDKDS ESFSEVC

-
Macromolecule #2: Condensin complex subunit 2

MacromoleculeName: Condensin complex subunit 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 86.323297 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
SequenceString: MTTQLRYENN DDDERVEYNL FTNRSTMMAN FEEWIKMATD NKINSRNSWN FALIDYFYDL DVLKDGENNI NFQKASATLD GCIKIYSSR VDSVTTETGK LLSGLAQRKT NGASNGDDSN GGNGEGLGGD SDEANIEIDP LTGMPISNDP DVNNTRRRVY N RVLETTLV ...String:
MTTQLRYENN DDDERVEYNL FTNRSTMMAN FEEWIKMATD NKINSRNSWN FALIDYFYDL DVLKDGENNI NFQKASATLD GCIKIYSSR VDSVTTETGK LLSGLAQRKT NGASNGDDSN GGNGEGLGGD SDEANIEIDP LTGMPISNDP DVNNTRRRVY N RVLETTLV EFETIKMKEL DQELIIDPLF KKALVDFDEG GAKSLLLNTL NIDNTARVIF DASIKDTQNV GQGKLQRKEE EL IERDSLV DDENEPSQSL ISTRNDSTVN DSVISAPSME DEILSLGMDF IKFDQIAVCE ISGSIEQLRN VVEDINQAKD FIE NVNNRF DNFLTEEELQ AAVPDNAEDD SDGFDMGMQQ ELCYPDENHD NTSHDEQDDD NVNSTTGSIF EKDLMAYFDE NLNR NWRGR EHWKVRNFKK ANLVNKESDL LEETRTTIGD TTDKNTTDDK SMDTKKKHKQ KKVLEIDFFK TDDSFEDKVF ASKGR TKID MPIKNRKNDT HYLLPDDFHF STDRITRLFI KPGQKMSLFS HRKHTRGDVS SGLFEKSTVS ANHSNNDIPT IADEHF WAD NYERKEQEEK EKEQSKEVGD VVGGALDNPF EDDMDGVDFN QAFEGTDDNE EASVKLDLQD DEDHKFPIRE NKVTYSR VS KKVDVRRLKK NVWRSINNLI QEHDSRKNRE QSSNDSETHT EDESTKELKF SDIIQGISKM YSDDTLKDIS TSFCFICL L HLANEHGLQI THTENYNDLI VNYEDLATTQ AAS

-
Macromolecule #3: DNA

MacromoleculeName: DNA / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 6.951477 KDa
SequenceString:
(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)(DT)

-
Macromolecule #4: DNA

MacromoleculeName: DNA / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 7.1588 KDa
SequenceString:
(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4)
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software: (Name: cryoSPARC, RELION)
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION
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 / Number images used: 91024

-
Atomic model buiding 1

Initial model
PDB IDChain

5oqq

chain_id: A

5oqq

chain_id: C

6zz6

chain_id: F

6zz6

chain_id: G
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-7q2z:
Cryo-EM structure of S.cerevisiae condensin Ycg1-Brn1-DNA complex

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more