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- EMDB-22697: CBF3 -

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Basic information

Entry
Database: EMDB / ID: EMD-22697
TitleCBF3
Map dataCBF3
Sample
  • Complex: CBF3CORE
    • Protein or peptide: Centromere DNA-binding protein complex CBF3 subunit C
    • Protein or peptide: Centromere DNA-binding protein complex CBF3 subunit B
  • Protein or peptide: Suppressor of kinetochore protein 1
KeywordsCBF3 / DNA BINDING PROTEIN
Function / homology
Function and homology information


RAVE complex / Iron uptake and transport / CBF3 complex / regulation of transcription by galactose / regulation of sulfur amino acid metabolic process / cellular response to methylmercury / vacuolar proton-transporting V-type ATPase complex assembly / septin ring assembly / centromeric DNA binding / regulation of exit from mitosis ...RAVE complex / Iron uptake and transport / CBF3 complex / regulation of transcription by galactose / regulation of sulfur amino acid metabolic process / cellular response to methylmercury / vacuolar proton-transporting V-type ATPase complex assembly / septin ring assembly / centromeric DNA binding / regulation of exit from mitosis / kinetochore assembly / vacuolar acidification / positive regulation of D-glucose transmembrane transport / protein neddylation / regulation of metabolic process / mitochondrial fusion / mitotic intra-S DNA damage checkpoint signaling / silent mating-type cassette heterochromatin formation / DNA binding, bending / exit from mitosis / SCF ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / mitotic spindle assembly checkpoint signaling / Orc1 removal from chromatin / DNA replication origin binding / cullin family protein binding / Antigen processing: Ubiquitination & Proteasome degradation / regulation of protein-containing complex assembly / subtelomeric heterochromatin formation / endomembrane system / negative regulation of cytoplasmic translation / regulation of mitotic cell cycle / kinetochore / G1/S transition of mitotic cell cycle / G2/M transition of mitotic cell cycle / mitotic cell cycle / ubiquitin-dependent protein catabolic process / protein-containing complex assembly / chromosome, telomeric region / DNA-binding transcription factor activity, RNA polymerase II-specific / protein ubiquitination / zinc ion binding / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Centromere DNA-binding protein complex CBF3 subunit B, C-terminal / : / Centromere DNA-binding protein complex CBF3 subunit B / Zn(2)-C6 fungal-type DNA-binding domain signature. / Fungal Zn(2)-Cys(6) binuclear cluster domain / Zn(2)-C6 fungal-type DNA-binding domain superfamily / Zn(2)-C6 fungal-type DNA-binding domain profile. / GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster DNA-binding domain / Zn(2)-C6 fungal-type DNA-binding domain / SKP1 component, dimerisation ...Centromere DNA-binding protein complex CBF3 subunit B, C-terminal / : / Centromere DNA-binding protein complex CBF3 subunit B / Zn(2)-C6 fungal-type DNA-binding domain signature. / Fungal Zn(2)-Cys(6) binuclear cluster domain / Zn(2)-C6 fungal-type DNA-binding domain superfamily / Zn(2)-C6 fungal-type DNA-binding domain profile. / GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster DNA-binding domain / Zn(2)-C6 fungal-type DNA-binding domain / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SKP1/BTB/POZ domain superfamily / Leucine-rich repeat domain superfamily
Similarity search - Domain/homology
Centromere DNA-binding protein complex CBF3 subunit C / Centromere DNA-binding protein complex CBF3 subunit B / Suppressor of kinetochore protein 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.0 Å
AuthorsRuifang G / Yawen B
CitationJournal: Nat Commun / Year: 2021
Title: Structural and dynamic mechanisms of CBF3-guided centromeric nucleosome formation.
Authors: Ruifang Guan / Tengfei Lian / Bing-Rui Zhou / Emily He / Carl Wu / Martin Singleton / Yawen Bai /
Abstract: Accurate chromosome segregation relies on the specific centromeric nucleosome-kinetochore interface. In budding yeast, the centromere CBF3 complex guides the deposition of CENP-A, an H3 variant, to ...Accurate chromosome segregation relies on the specific centromeric nucleosome-kinetochore interface. In budding yeast, the centromere CBF3 complex guides the deposition of CENP-A, an H3 variant, to form the centromeric nucleosome in a DNA sequence-dependent manner. Here, we determine the structures of the centromeric nucleosome containing the native CEN3 DNA and the CBF3core bound to the canonical nucleosome containing an engineered CEN3 DNA. The centromeric nucleosome core structure contains 115 base pair DNA including a CCG motif. The CBF3core specifically recognizes the nucleosomal CCG motif through the Gal4 domain while allosterically altering the DNA conformation. Cryo-EM, modeling, and mutational studies reveal that the CBF3core forms dynamic interactions with core histones H2B and CENP-A in the CEN3 nucleosome. Our results provide insights into the structure of the budding yeast centromeric nucleosome and the mechanism of its assembly, which have implications for analogous processes of human centromeric nucleosome formation.
History
DepositionSep 22, 2020-
Header (metadata) releaseMar 31, 2021-
Map releaseMar 31, 2021-
UpdateOct 30, 2024-
Current statusOct 30, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7k79
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22697.png

Downloads & links

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Map

FileDownload / File: emd_22697.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCBF3
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 280 pix.
= 296.8 Å		1.06 Å/pix.
x 280 pix.
= 296.8 Å		1.06 Å/pix.
x 280 pix.
= 296.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02 / Movie #1: 0.02
Minimum - Maximum-0.020057408 - 0.05685778
Average (Standard dev.)0.00016743768 (±0.0022741188)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 296.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.061.061.06
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z296.800296.800296.800
α/β/γ90.00090.00090.000
start NX/NY/NZ15150
NX/NY/NZ9999114
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.0200.0570.000

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Supplemental data

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Sample components

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Entire : CBF3CORE

EntireName: CBF3CORE
Components
  • Complex: CBF3CORE
    • Protein or peptide: Centromere DNA-binding protein complex CBF3 subunit C
    • Protein or peptide: Centromere DNA-binding protein complex CBF3 subunit B
  • Protein or peptide: Suppressor of kinetochore protein 1

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Supramolecule #1: CBF3CORE

SupramoleculeName: CBF3CORE / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: Centromere DNA-binding protein complex CBF3 subunit C

MacromoleculeName: Centromere DNA-binding protein complex CBF3 subunit C / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 60.899961 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MGPSFNPVRF LELPIDIRKE VYFHLDGNFC GAHPYPIDIL YKSNDVELPG KPSYKRSKRS KKLLRYMYPV FATYLNIFEY SPQLIEKWL EYAFWLRYDC LVLDCFKVNH LYDGTLIDAL EWTYLDNELR LAYFNKASML EVWYTFKEYK KWVIDSVAFD E LDLLNVSN ...String:
MGPSFNPVRF LELPIDIRKE VYFHLDGNFC GAHPYPIDIL YKSNDVELPG KPSYKRSKRS KKLLRYMYPV FATYLNIFEY SPQLIEKWL EYAFWLRYDC LVLDCFKVNH LYDGTLIDAL EWTYLDNELR LAYFNKASML EVWYTFKEYK KWVIDSVAFD E LDLLNVSN IQFNIDNLTP QLVDKCLSIL EQKDLFATIG EVQFGQDEEV GEEKDVDVSG ANSDENSSPS STIKNKKRSA SK RSHSDNG NVGATHNQLT SISVIRTIRS MESMKSLRKI TVRGEKLYEL LINFHGFRDN PGKTISYIVK RRINEIRLSR MNQ ISRTGL ADFTRWDNLQ KLVLSRVAYI DLNSIVFPKN FKSLTMKRVS KIKWWNIEEN ILKELKVDKR TFKSLYIKED DSKF TKFFN LRHTRIKELD KSEINQITYL RCQAIVWLSF RTLNHIKLQN VSEVFNNIIV PRALFDSKRV EIYRCEKISQ VLVIG SRSG SENLYFQGSK RRWKKNFIAV SAANRFKKIS SSGAL

UniProtKB: Centromere DNA-binding protein complex CBF3 subunit C

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Macromolecule #2: Centromere DNA-binding protein complex CBF3 subunit B

MacromoleculeName: Centromere DNA-binding protein complex CBF3 subunit B / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 72.637117 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MFNRTTQLKS KHPCSVCTRR KVKCDRMIPC GNCRKRGQDS ECMKSTKLIT ASSSKEYLPD LLLFWQNYEY WITNIGLYKT KQRDLTRTP ANLDTDTEEC MFWMNYLQKD QSFQLMNFAM ENLGALYFGS IGDISELYLR VEQYWDRRAD KNHSVDGKYW D ALIWSVFT ...String:
MFNRTTQLKS KHPCSVCTRR KVKCDRMIPC GNCRKRGQDS ECMKSTKLIT ASSSKEYLPD LLLFWQNYEY WITNIGLYKT KQRDLTRTP ANLDTDTEEC MFWMNYLQKD QSFQLMNFAM ENLGALYFGS IGDISELYLR VEQYWDRRAD KNHSVDGKYW D ALIWSVFT MCIYYMPVEK LAEIFSVYPL HEYLGSNKRL NWEDGMQLVM CQNFARCSLF QLKQCDFMAH PDIRLVQAYL IL ATTTFPY DEPLLANSLL TQCIHTFKNF HVDDFRPLLN DDPVESIAKV TLGRIFYRLC GCDYLQSGPR KPIALHTEVS SLL QHAAYL QDLPNVDVYR EENSTEVLYW KIISLDRDLD QYLNKSSKPP LKTLDAIRRE LDIFQYKVDS LEEDFRSNNS RFQK FIALF QISTVSWKLF KMYLIYYDTA DSLLKVIHYS KVIISLIVNN FHAKSEFFNR HPMVMQTITR VVSFISFYQI FVESA AVKQ LLVDLTELTA NLPTIFGSKL DKLVYLTERL SKLKLLWDKV QLLDSGDSFY HPVFKILQND IKIIELKNDE MFSLIK GLG SLVPLNKLRQ ESLLEEEDEN NTEPSDFRTI VEEFQSEYNI SDILSGSGGS GENLYFQ

UniProtKB: Centromere DNA-binding protein complex CBF3 subunit B

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Macromolecule #3: Suppressor of kinetochore protein 1

MacromoleculeName: Suppressor of kinetochore protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 22.35727 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MVTSNVVLVS GEGERFTVDK KIAERSLLLK NYLNDMHDSN LQNNSDSESD SDSETNHKSK DNNNGDDDDE DDDEIVMPVP NVRSSVLQK VIEWAEHHRD SNFPDEDDDD SRKSAPVDSW DREFLKVDQE MLYEIILAAN YLNIKPLLDA GCKVVAEMIR G RSPEEIRR ...String:
MVTSNVVLVS GEGERFTVDK KIAERSLLLK NYLNDMHDSN LQNNSDSESD SDSETNHKSK DNNNGDDDDE DDDEIVMPVP NVRSSVLQK VIEWAEHHRD SNFPDEDDDD SRKSAPVDSW DREFLKVDQE MLYEIILAAN YLNIKPLLDA GCKVVAEMIR G RSPEEIRR TFNIVNDFTP EEEAAIRREN EWAEDR

UniProtKB: Suppressor of kinetochore protein 1

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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

BufferpH: 7.3
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 71.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 115666
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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