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Open data
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Basic information
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Title | Cryo-EM structure of 5-subunit Smc5/6 | |||||||||
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![]() | CELL CYCLE | |||||||||
Function / homology | ![]() 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 / ATPase inhibitor activity / chromatin looping / protein serine/threonine kinase inhibitor activity / Transferases; Acyltransferases; Aminoacyltransferases ...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 / ATPase inhibitor activity / 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 | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.5 Å | |||||||||
![]() | Qian L / Jun Z / Xiang Z / Zhaoning W / Tong C / Duo J / Zhenguo C / Wang LF | |||||||||
Funding support | 1 items
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![]() | ![]() 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 |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 563.7 KB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.9 KB 17.9 KB | Display Display | ![]() |
Images | ![]() | 47.6 KB | ||
Filedesc metadata | ![]() | 7.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 305.3 KB | Display | ![]() |
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Full document | ![]() | 304.8 KB | Display | |
Data in XML | ![]() | 6.1 KB | Display | |
Data in CIF | ![]() | 7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8i4xMC ![]() 7ylmC ![]() 7ymdC ![]() 7yqhC ![]() 8hqsC ![]() 8i13C ![]() 8i21C ![]() 8i4uC ![]() 8i4vC ![]() 8i4wC ![]() 8wjlC ![]() 8wjnC ![]() 8wjoC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 2.128 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Cryo-EM structure of 5-subunit Smc5/6
Entire | Name: Cryo-EM structure of 5-subunit Smc5/6 |
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Components |
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-Supramolecule #1: Cryo-EM structure of 5-subunit Smc5/6
Supramolecule | Name: Cryo-EM structure of 5-subunit Smc5/6 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Structural maintenance of chromosomes protein 5
Macromolecule | Name: Structural maintenance of chromosomes protein 5 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 123.390031 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: 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 |
-Macromolecule #2: Structural maintenance of chromosomes protein 6
Macromolecule | Name: Structural maintenance of chromosomes protein 6 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 126.889375 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: 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 VNNSLVVSAQ 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 IHRMRDP UniProtKB: Structural maintenance of chromosomes protein 6 |
-Macromolecule #3: E3 SUMO-protein ligase MMS21
Macromolecule | Name: E3 SUMO-protein ligase MMS21 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO EC number: Transferases; Acyltransferases; Aminoacyltransferases |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 30.388336 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MALNDNPIPK SVPLHPKSGK YFHNLHARDL SNIYQQCYKQ IDETINQLVD STSPSTIGIE EQVADITSTY KLLSTYESES NSFDEHIKD LKKNFKQSSD ACPQIDLSTW DKYRTGELTA PKLSELYLNM PTPEPATMVN NTDTLKILKV LPYIWNDPTC V IPDLQNPA ...String: MALNDNPIPK SVPLHPKSGK YFHNLHARDL SNIYQQCYKQ IDETINQLVD STSPSTIGIE EQVADITSTY KLLSTYESES NSFDEHIKD LKKNFKQSSD ACPQIDLSTW DKYRTGELTA PKLSELYLNM PTPEPATMVN NTDTLKILKV LPYIWNDPTC V IPDLQNPA DEDDLQIEGG KIELTCPITC KPYEAPLISR KCNHVFDRDG IQNYLQGYTT RDCPQAACSQ VVSMRDFVRD PI MELRCKI AKMKESQEQD KRSSQAIDVL UniProtKB: E3 SUMO-protein ligase MMS21 |
-Macromolecule #4: Nse6
Macromolecule | Name: Nse6 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 44.498242 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: PILKRTIISK RKAPSNNEDE EIVKTPRKLV NYVPLKIFNL GDSFDDTITT TVAKLQDLKK EILDSPRSNK SIVITSNTVA KSELQKSIK FSGSIPEIYL DVVTKETISD KYKDWHFISK NCHYEQLMDL EMKDTAYSFL FGSSRSQGKV PEFVHLKCPS I TNLLVLFG ...String: PILKRTIISK RKAPSNNEDE EIVKTPRKLV NYVPLKIFNL GDSFDDTITT TVAKLQDLKK EILDSPRSNK SIVITSNTVA KSELQKSIK FSGSIPEIYL DVVTKETISD KYKDWHFISK NCHYEQLMDL EMKDTAYSFL FGSSRSQGKV PEFVHLKCPS I TNLLVLFG VNQEKCNSLK INYEKKENSR YDNLCTIFPV NKMLKFLMYF YSDDDNDDVR EFFLKAFICL ILDRKVFNAM ES DHRLCFK VLELFNEAHF INSYFEIVDK NDFFLHYRLL QIFPHLQSAL LRRRFSEKQG RTETIQQNII KEFNEFFDCK NYK NLLYFI LTMYGSKFIP FGPKCQVTEY FKDCILDISN ETTNDVEISI LKGILNLFSK IR UniProtKB: DNA repair protein KRE29 |
-Macromolecule #5: Non-structural maintenance of chromosome element 5
Macromolecule | Name: Non-structural maintenance of chromosome element 5 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 64.079609 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MDGALINSVL YVSPRNGAHY FVELTEKHLL AFEMLNSMCL LENYDHVLLF LECQFGKSHN LAVIPFDIIL VLFTLSTLSE YYKEPILRA NDPYNTSRET LSRRALKLLQ KYLAILKEFD SEQYNLYDLE LLRCQFFLAI DTLTPKKQKW GFDRFRRTKS E SGVTYRQN ...String: MDGALINSVL YVSPRNGAHY FVELTEKHLL AFEMLNSMCL LENYDHVLLF LECQFGKSHN LAVIPFDIIL VLFTLSTLSE YYKEPILRA NDPYNTSRET LSRRALKLLQ KYLAILKEFD SEQYNLYDLE LLRCQFFLAI DTLTPKKQKW GFDRFRRTKS E SGVTYRQN ASVDPELDQA KTFKNPYRSY ISCLEQRNTI LGNRLLNLKL NEPGEFINMI LWTLSNSLQE STPLFLSSHE IW MPLLEIL IDLFSCRQDY FIQHEVAQNV SKSLFVQRLS ESPLAVFFES LNTRNFANRF SEYVFLNCDY KLPSDNYATP VHP VYNGEN TIVDTYIPTI KCSPLYKSQK SLALRRKLIG SCFKLLLRVP DGHRLITPRI VADDVIQGIS RTLASFNDIL QFKK FFMTE NLSQESYFIP LLAEGTLSEI LKDTQECVVI LTLVENLSDG VSFCNEVIGL VKSKCFAFTE QCSQASYEEA VLNIE KCDV CLLVLLRYLL HLIGTEAILD AKEQLEMLHA IEKNDSGRRQ WAKALNLGND PPLLYPIVSQ MFGVHDKSVI IE UniProtKB: Non-structural maintenance of chromosome element 5 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination 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 model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 8.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 268567 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |