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- EMDB-35185: Cryo-EM structure of 5-subunit Smc5/6 arm region -

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Basic information

Entry
Database: EMDB / ID: EMD-35185
TitleCryo-EM structure of 5-subunit Smc5/6 arm region
Map data
Sample
  • Complex: Cryo-EM structure of 5-subunit Smc5/6 arm region
    • Protein or peptide: Structural maintenance of chromosomes protein 5
    • Protein or peptide: Structural maintenance of chromosomes protein 6
    • Protein or peptide: E3 SUMO-protein ligase MMS21
    • Protein or peptide: DNA repair protein KRE29
KeywordsCELL CYCLE
Function / homology
Function and homology information


Smc5-Smc6 complex / resolution of DNA recombination intermediates / DNA double-strand break attachment to nuclear envelope / chromosome separation / SUMO ligase activity / SUMOylation of DNA damage response and repair proteins / chromatin looping / protein serine/threonine kinase inhibitor activity / Transferases; Acyltransferases; Aminoacyltransferases / SUMO transferase activity ...Smc5-Smc6 complex / resolution of DNA recombination intermediates / DNA double-strand break attachment to nuclear envelope / chromosome separation / SUMO ligase activity / SUMOylation of DNA damage response and repair proteins / chromatin looping / protein serine/threonine kinase inhibitor activity / Transferases; Acyltransferases; Aminoacyltransferases / SUMO transferase activity / recombinational repair / regulation of telomere maintenance / protein sumoylation / double-strand break repair via homologous recombination / nuclear envelope / site of double-strand break / single-stranded DNA binding / chromosome, telomeric region / damaged DNA binding / DNA repair / ATP hydrolysis activity / mitochondrion / zinc ion binding / ATP binding / nucleus / cytoplasm
Similarity search - Function
DNA repair protein Nse5/Nse6 / DNA repair proteins Nse5 and Nse6 / E3 SUMO-protein ligase Nse2 (Mms21) / Zinc-finger of the MIZ type in Nse subunit / Structural maintenance of chromosomes protein 5 / Zinc finger, MIZ-type / Zinc finger SP-RING-type profile. / Rad50/SbcC-type AAA domain / AAA domain / RecF/RecN/SMC, N-terminal ...DNA repair protein Nse5/Nse6 / DNA repair proteins Nse5 and Nse6 / E3 SUMO-protein ligase Nse2 (Mms21) / Zinc-finger of the MIZ type in Nse subunit / Structural maintenance of chromosomes protein 5 / Zinc finger, MIZ-type / Zinc finger SP-RING-type profile. / Rad50/SbcC-type AAA domain / AAA domain / RecF/RecN/SMC, N-terminal / RecF/RecN/SMC N terminal domain / Zinc finger, RING/FYVE/PHD-type / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
E3 SUMO-protein ligase MMS21 / DNA repair protein KRE29 / Structural maintenance of chromosomes protein 5 / Structural maintenance of chromosomes protein 6
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 5.97 Å
AuthorsQian L / Jun Z / Xiang Z / Cheng T / Zhaoning W / Zhenguo C / Wang L
Funding support1 items
OrganizationGrant numberCountry
Other government
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Cryo-EM structures of Smc5/6 in multiple states reveal its assembly and functional mechanisms.
Authors: Qian Li / Jun Zhang / Cory Haluska / Xiang Zhang / Lei Wang / Guangfeng Liu / Zhaoning Wang / Duo Jin / Tong Cheng / Hongxia Wang / Yuan Tian / Xiangxi Wang / Lei Sun / Xiaolan Zhao / ...Authors: Qian Li / Jun Zhang / Cory Haluska / Xiang Zhang / Lei Wang / Guangfeng Liu / Zhaoning Wang / Duo Jin / Tong Cheng / Hongxia Wang / Yuan Tian / Xiangxi Wang / Lei Sun / Xiaolan Zhao / Zhenguo Chen / Lanfeng Wang /
Abstract: Smc5/6 is a member of the eukaryotic structural maintenance of chromosomes (SMC) family of complexes with important roles in genome maintenance and viral restriction. However, limited structural ...Smc5/6 is a member of the eukaryotic structural maintenance of chromosomes (SMC) family of complexes with important roles in genome maintenance and viral restriction. However, limited structural understanding of Smc5/6 hinders the elucidation of its diverse functions. Here, we report cryo-EM structures of the budding yeast Smc5/6 complex in eight-subunit, six-subunit and five-subunit states. Structural maps throughout the entire length of these complexes reveal modularity and key elements in complex assembly. We show that the non-SMC element (Nse)2 subunit supports the overall shape of the complex and uses a wedge motif to aid the stability and function of the complex. The Nse6 subunit features a flexible hook region for attachment to the Smc5 and Smc6 arm regions, contributing to the DNA repair roles of the complex. Our results also suggest a structural basis for the opposite effects of the Nse1-3-4 and Nse5-6 subcomplexes in regulating Smc5/6 ATPase activity. Collectively, our integrated structural and functional data provide a framework for understanding Smc5/6 assembly and function.
History
DepositionJan 21, 2023-
Header (metadata) releaseJun 26, 2024-
Map releaseJun 26, 2024-
UpdateJul 3, 2024-
Current statusJul 3, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35185.png

Downloads & links

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Map

FileDownload / File: emd_35185.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 2.128 Å
Density
Contour LevelBy AUTHOR: 0.5
Minimum - Maximum-5.5624475 - 8.602857999999999
Average (Standard dev.)-0.00086631684 (±0.055287283)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 680.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_35185_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_35185_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Cryo-EM structure of 5-subunit Smc5/6 arm region

EntireName: Cryo-EM structure of 5-subunit Smc5/6 arm region
Components
  • Complex: Cryo-EM structure of 5-subunit Smc5/6 arm region
    • Protein or peptide: Structural maintenance of chromosomes protein 5
    • Protein or peptide: Structural maintenance of chromosomes protein 6
    • Protein or peptide: E3 SUMO-protein ligase MMS21
    • Protein or peptide: DNA repair protein KRE29

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Supramolecule #1: Cryo-EM structure of 5-subunit Smc5/6 arm region

SupramoleculeName: Cryo-EM structure of 5-subunit Smc5/6 arm region / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: Structural maintenance of chromosomes protein 5

MacromoleculeName: Structural maintenance of chromosomes protein 5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 123.390031 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: KRVKIAKPDL SSFQPGSIIK IRLQDFVTYT LTEFNLSPSL NMIIGPNGSG KSTFVCAVCL GLAGKPEYIG RSKKVEDFIK NGQDVSKIE ITLKNSPNVT DIEYIDARDE TIKITRIITR SKRRSDYLIN DYQVSESVVK TLVAQLNIQL DNLCQFLSQE R VEEFARLK ...String:
KRVKIAKPDL SSFQPGSIIK IRLQDFVTYT LTEFNLSPSL NMIIGPNGSG KSTFVCAVCL GLAGKPEYIG RSKKVEDFIK NGQDVSKIE ITLKNSPNVT DIEYIDARDE TIKITRIITR SKRRSDYLIN DYQVSESVVK TLVAQLNIQL DNLCQFLSQE R VEEFARLK SVKLLVETIR SIDASLLDVL DELRELQGNE QSLQKDLDFK KAKIVHLRQE SDKLRKSVES LRDFQNKKGE IE LHSQLLP YVKVKDHKEK LNIYKEEYER AKANLRAILK DKKPFANTKK TLENQVEELT EKCSLKTDEF LKAKEKINEI FEK LNTIRD EVIKKKNQNE YYRGRTKKLQ ATIISTKEDF LRSQEILAQT HLPEKSVFED IDIKRKEIIN KEGEIRDLIS EIDA KANAI NHEMRSIQRQ AESKTKSLTT TDKIGILNQD QDLKEVRDAV LMVREHPEMK DKILEPPIMT VSAINAQFAA YLAQC VDYN TSKALTVVDS DSYKLFANPI LDKFKVNLRE LSSADTTPPV PAETVRDLGF EGYLSDFITG DKRVMKMLCQ TSKIHT IPV SRRELTPAQI KKLITPRPNG KILFKRIIHG NRLVDIKQSA YGSKQVFPTD VSIKQTNFYQ GSIMSNEQKI RIENEII NL KNEYNDRKST LDALSNQKSG YRHELSELAS KNDDINREAH QLNEIRKKYT MRKSTIETLR EKLDQLKREA RKDVSQKI K DIDDQIQQLL LKQRHLLSKM ASSMKSLKNC QKELISTQIL QFEAQNMDVS MNDVIGFFNE READLKSQYE DKKKFVKEA RDTPEFQSWM REIRSYDQDT KEKLNKVAEK YEEEGNFNLS FVQDVLDKLE SEIAMVNHDE SAVTILDQVT AELRELEHTV PQQSKDLET IKAKLKEDHA VLEPKLDDIV SKISARFARL FNNVGSAGAV RLEKPKDYAE WKIEIMVKFR DNAPLKKLDS H TQSGGERA VSTVLYMIAL QEFTSAPFRV VDEINQGMDS RNERIVHKAM VENACAENTS QYFLITPKLL TGLHYHEKMR IH CVMAGSW IPNPSEDPKM IHFGETSNYS FD

UniProtKB: Structural maintenance of chromosomes protein 5

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Macromolecule #2: Structural maintenance of chromosomes protein 6

MacromoleculeName: Structural maintenance of chromosomes protein 6 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 128.199727 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MISTTISGKR PIEQVDDELL SLTAQQENEE QQQQRKRRRH QFAPMTQFNS NTLDEDSGFR SSSDVATADQ DNFLEESPSG YIKKVILRN FMCHEHFELE LGSRLNFIVG NNGSGKSAIL TAITIGLGAK ASETNRGSSL KDLIREGCYS AKIILHLDNS K YGAYQQGI ...String:
MISTTISGKR PIEQVDDELL SLTAQQENEE QQQQRKRRRH QFAPMTQFNS NTLDEDSGFR SSSDVATADQ DNFLEESPSG YIKKVILRN FMCHEHFELE LGSRLNFIVG NNGSGKSAIL TAITIGLGAK ASETNRGSSL KDLIREGCYS AKIILHLDNS K YGAYQQGI FGNEIIVERI IKRDGPASFS LRSENGKEIS NKKKDIQTVV DYFSVPVSNP MCFLSQDAAR SFLTASTSQD KY SHFMKGT LLQEITENLL YASAIHDSAQ ENMALHLENL KSLKAEYEDA KKLLRELNQT SDLNERKMLL QAKSLWIDVA HNT DACKNL ENEISGIQQK VDEVTEKIRN RQEKIERYTS DGTTIEAQID AKVIYVNEKD SEHQNARELL RDVKSRFEKE KSNQ AEAQS NIDQGRKKVD ALNKTIAHLE EELTKEMGGD KDQMRQELEQ LEKANEKLRE VNNSLVVSLQ DVKNEERDIQ HERES ELRT ISRSIQNKKV ELQNIAKGND TFLMNFDRNM DRLLRTIEQR KNEFETPAIG PLGSLVTIRK GFEKWTRSIQ RAISSS LNA FVVSNPKDNR LFRDIMRSCG IRSNIPIVTY CLSQFDYSKG RAHGNYPTIV DALEFSKPEI ECLFVDLSRI ERIVLIE DK NEARNFLQRN PVNVNMALSL RDRRSGFQLS GGYRLDTVTY QDKIRLKVNS SSDNGTQYLK DLIEQETKEL QNIRDRYE E KLSEVRSRLK EIDGRLKSTK NEMRKTNFRM TELKMNVGKV VDTGILNSKI NERKNQEQAI ASYEAAKEEL GLKIEQIAQ EAQPIKEQYD STKLALVEAQ DELQQLKEDI NSRQSKIQKY KDDTIYYEDK KKVYLENIKK IEVNVAALKE GIQRQIQNAC AFCSKERIE NVDLPDTQEE IKRELDKVSR MIQKAEKSLG LSQEEVIALF EKCRNKYKEG QKKYMEIDEA LNRLHNSLKA R DQNYKNAE KGTCFDADMD FRASLKVRKF SGNLSFIKDT KSLEIYILTT NDEKARNVDT LSGGEKSFSQ MALLLATWKP MR SRIIALD EFDVFMDQVN RKIGTTLIVK KLKDIARTQT IIITPQDIGK IADIDSSGVS IHRMRDPERQ NNSNFYN

UniProtKB: Structural maintenance of chromosomes protein 6

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Macromolecule #3: E3 SUMO-protein ligase MMS21

MacromoleculeName: E3 SUMO-protein ligase MMS21 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
EC number: Transferases; Acyltransferases; Aminoacyltransferases
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 28.600305 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: NDNPIPKSVP LHPKSGKYFH NLHARDLSNI YQQCYKQIDE TINQLVDSTS PSTIGIEEQV ADITSTYKLL STYESESNSF DEHIKDLKK NFKQSSDACP QIDLSTWDKY RTGELTAPKL SELYLNMPTP EPATMVNNTD TLKILKVLPY IWNDPTCVIP D LQNPADED ...String:
NDNPIPKSVP LHPKSGKYFH NLHARDLSNI YQQCYKQIDE TINQLVDSTS PSTIGIEEQV ADITSTYKLL STYESESNSF DEHIKDLKK NFKQSSDACP QIDLSTWDKY RTGELTAPKL SELYLNMPTP EPATMVNNTD TLKILKVLPY IWNDPTCVIP D LQNPADED DLQIEGGKIE LTCPITCKPY EAPLISRKCN HVFDRDGIQN YLQGYTTRDC PQAACSQVVS MRDFVRDPIM EL RCKIAKM KESQ

UniProtKB: E3 SUMO-protein ligase MMS21

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Macromolecule #4: DNA repair protein KRE29

MacromoleculeName: DNA repair protein KRE29 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 7.337511 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
PILKRTIISK RKAPSNNEDE EIVKTPRKLV NYVPLKIFNL GDSFDDTITT TVAKLQDLKK EILD

UniProtKB: DNA repair protein KRE29

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: DARK FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 5.97 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 227122
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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