[English] 日本語
Yorodumi
- EMDB-29413: EM map of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-29413
TitleEM map of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a 10-nt gapped DNA in step 2 (open 9-1-1 ring and flexibly bound chamber DNA)
Map dataEM map of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a 10-nt gapped DNA in step 2 (open 9-1-1 ring and flexibly bound chamber DNA)
Sample
  • Complex: Rad24-RFC-911 clamp-DNA
    • Complex: DNA
      • DNA: x 3 types
    • Complex: Proteins complex
      • Protein or peptide: x 3 types
  • Protein or peptide: x 5 types
  • Ligand: x 3 types
KeywordsDNA damage repair / Rad24-RFC / 9-1-1 clamp / DNA clamp / alternative clamp loader / DNA damage signaling / DNA BINDING PROTEIN-DNA complex / CELL CYCLE-DNA complex
Function / homology
Function and homology information


meiotic DNA integrity checkpoint signaling / checkpoint clamp complex / Rad17 RFC-like complex / Gap-filling DNA repair synthesis and ligation in GG-NER / Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / Polymerase switching / DNA clamp loader activity / Translesion synthesis by REV1 ...meiotic DNA integrity checkpoint signaling / checkpoint clamp complex / Rad17 RFC-like complex / Gap-filling DNA repair synthesis and ligation in GG-NER / Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / Polymerase switching / DNA clamp loader activity / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Translesion Synthesis by POLH / DNA replication checkpoint signaling / Termination of translesion DNA synthesis / Activation of ATR in response to replication stress / telomere maintenance via recombination / mitotic DNA replication checkpoint signaling / reciprocal meiotic recombination / mitotic intra-S DNA damage checkpoint signaling / recombinational repair / sister chromatid cohesion / mitotic sister chromatid cohesion / leading strand elongation / Gap-filling DNA repair synthesis and ligation in TC-NER / Dual incision in TC-NER / subtelomeric heterochromatin formation / mismatch repair / 3'-5' exonuclease activity / telomere maintenance / DNA damage checkpoint signaling / cellular response to ionizing radiation / meiotic cell cycle / nucleotide-excision repair / double-strand break repair via homologous recombination / DNA-templated DNA replication / double-strand break repair / site of double-strand break / double-stranded DNA binding / damaged DNA binding / chromosome, telomeric region / DNA repair / chromatin binding / ATP hydrolysis activity / DNA binding / ATP binding / nucleus / cytosol
Similarity search - Function
Ddc1 / DNA damage checkpoint control protein Rad17 / Rad17 P-loop domain / Checkpoint protein Hus1/Mec3 / Hus1-like protein / Checkpoint protein Rad17/Rad24 / Checkpoint protein Rad17/Rad24, fungi/metazoa / Rad1/Rec1/Rad17 / Rad9/Ddc1 / Repair protein Rad1/Rec1/Rad17 ...Ddc1 / DNA damage checkpoint control protein Rad17 / Rad17 P-loop domain / Checkpoint protein Hus1/Mec3 / Hus1-like protein / Checkpoint protein Rad17/Rad24 / Checkpoint protein Rad17/Rad24, fungi/metazoa / Rad1/Rec1/Rad17 / Rad9/Ddc1 / Repair protein Rad1/Rec1/Rad17 / RFC1-like, AAA+ ATPase lid domain / Replication factor C subunit 3, C-terminal domain / RCF1/5-like, AAA+ ATPase lid domain / Replication factor C, C-terminal / Replication factor C C-terminal domain / : / DNA polymerase III, delta subunit / : / DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal / : / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DDC1 isoform 1 / DNA damage checkpoint control protein RAD17 / Checkpoint protein RAD24 / Replication factor C subunit 5 / Replication factor C subunit 3 / Replication factor C subunit 4 / Replication factor C subunit 2 / DNA damage checkpoint control protein MEC3
Similarity search - Component
Biological speciessynthetic construct (others) / Saccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.94 Å
AuthorsZheng F / Georgescu R / Yao YN / O'Donnell ME / Li H
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM131754 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM115809 United States
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: bioRxiv / Year: 2023
Title: Structures of 9-1-1 DNA checkpoint clamp loading at gaps from start to finish and ramification to biology.
Authors: Fengwei Zheng / Roxana E Georgescu / Nina Y Yao / Michael E O'Donnell / Huilin Li /
Abstract: Recent structural studies show the Rad24-RFC loads the 9-1-1 checkpoint clamp onto a recessed 5' end by binding the 5' DNA on Rad24 at an external surface site and threading the 3' ssDNA into the ...Recent structural studies show the Rad24-RFC loads the 9-1-1 checkpoint clamp onto a recessed 5' end by binding the 5' DNA on Rad24 at an external surface site and threading the 3' ssDNA into the well-established internal chamber and into 9-1-1. We find here that Rad24-RFC loads 9-1-1 onto DNA gaps in preference to a recessed 5' DNA end, thus presumably leaving 9-1-1 on a 3' ss/ds DNA after Rad24-RFC ejects from the 5' gap end and may explain reports of 9-1-1 directly functioning in DNA repair with various TLS polymerases, in addition to signaling the ATR kinase. To gain a deeper understanding of 9-1-1 loading at gaps we report high-resolution structures of Rad24-RFC during loading of 9-1-1 onto 10-nt and 5-nt gapped DNAs. At a 10-nt gap we captured five Rad24-RFC-9-1-1 loading intermediates in which the 9-1-1 DNA entry gate varies from fully open to fully closed around DNA using ATPγS, supporting the emerging view that ATP hydrolysis is not needed for clamp opening/closing, but instead for dissociation of the loader from the clamp encircling DNA. The structure of Rad24-RFC-9-1-1 at a 5-nt gap shows a 180° axially rotated 3'-dsDNA which orients the template strand to bridge the 3'- and 5'- junctions with a minimum 5-nt ssDNA. The structures reveal a unique loop on Rad24 that limits the length of dsDNA in the inner chamber, and inability to melt DNA ends unlike RFC, thereby explaining Rad24-RFC's preference for a preexisting ssDNA gap and suggesting a direct role in gap repair in addition to its checkpoint role.
History
DepositionJan 9, 2023-
Header (metadata) releaseJun 14, 2023-
Map releaseJun 14, 2023-
UpdateJun 4, 2025-
Current statusJun 4, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_29413.png

Downloads & links

-
Map

FileDownload / File: emd_29413.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationEM map of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a 10-nt gapped DNA in step 2 (open 9-1-1 ring and flexibly bound chamber DNA)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 420 pix.
= 347.76 Å		0.83 Å/pix.
x 420 pix.
= 347.76 Å		0.83 Å/pix.
x 420 pix.
= 347.76 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.828 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.12
Minimum - Maximum-0.9865499 - 1.499062
Average (Standard dev.)-0.00019707673 (±0.02788455)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions420420420
Spacing420420420
CellA=B=C: 347.76 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: half map B

Fileemd_29413_half_map_1.map
Annotationhalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: half map A

Fileemd_29413_half_map_2.map
Annotationhalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : Rad24-RFC-911 clamp-DNA

EntireName: Rad24-RFC-911 clamp-DNA
Components
  • Complex: Rad24-RFC-911 clamp-DNA
    • Complex: DNA
      • DNA: Template strand
      • DNA: Primer strand 1
      • DNA: Primer strand 2
    • Complex: Proteins complex
      • Protein or peptide: DNA damage checkpoint control protein MEC3
      • Protein or peptide: DNA damage checkpoint control protein RAD17
      • Protein or peptide: DDC1 isoform 1
  • Protein or peptide: Checkpoint protein RAD24
  • Protein or peptide: Replication factor C subunit 4
  • Protein or peptide: Replication factor C subunit 3
  • Protein or peptide: Replication factor C subunit 2
  • Protein or peptide: Replication factor C subunit 5
  • Ligand: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

+
Supramolecule #1: Rad24-RFC-911 clamp-DNA

SupramoleculeName: Rad24-RFC-911 clamp-DNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #6-#11

+
Supramolecule #2: DNA

SupramoleculeName: DNA / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #9-#11 / Details: synthetic DNA
Source (natural)Organism: synthetic construct (others) / Synthetically produced: Yes

+
Supramolecule #3: Proteins complex

SupramoleculeName: Proteins complex / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #6-#8
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

+
Macromolecule #1: Checkpoint protein RAD24

MacromoleculeName: Checkpoint protein RAD24 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 62.721418 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MDSTNLNKRP LLQYSLSSLG SQITKWSSSR PTSPVRKARS TENDFLSKQD TSSILPSIND DGGEQWYEKF KPNCLEQVAI HKRKLKDVQ EALDAMFLPN AKHRILLLSG PSGCSKSTVI KELSKILVPK YRQNSNGTSF RSTPNEHKVT EFRGDCIVND L PQMESFSE ...String:
MDSTNLNKRP LLQYSLSSLG SQITKWSSSR PTSPVRKARS TENDFLSKQD TSSILPSIND DGGEQWYEKF KPNCLEQVAI HKRKLKDVQ EALDAMFLPN AKHRILLLSG PSGCSKSTVI KELSKILVPK YRQNSNGTSF RSTPNEHKVT EFRGDCIVND L PQMESFSE FLKGARYLVM SNLSLILIED LPNVFHIDTR RRFQQLILQW LYSSEPLLPP LVICITECEI PENDNNYRKF GI DYTFSAE TIMNKEILMH PRLKRIKFNP INSTLLKKHL KFICVQNMKM LKEKNKWNKR QEVIDYIAQE TGDIRSAITT LQF WATSSG SLPISTREST ISYFHAIGKV IHGSHSTNND NEMINNLFEN SNNLLSKEDF KLGILENYNT FNKGEFSISD ASSI VDCLS ECDNMNGLPE SNEYGLREVR KTFRNISKQG HNHGTVYFPR EWKVRKLQNS FKVQAEDWLN VSLYKYNAVH SFRNI TLEF GYYAPLIRKC QSYKKKYILY YLKNLPSGSS GPKQTMDKFS DIMKVENGID VVDRIGGPIE

UniProtKB: Checkpoint protein RAD24

+
Macromolecule #2: Replication factor C subunit 4

MacromoleculeName: Replication factor C subunit 4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 36.201039 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSKTLSLQLP WVEKYRPQVL SDIVGNKETI DRLQQIAKDG NMPHMIISGM PGIGKTTSVH CLAHELLGRS YADGVLELNA SDDRGIDVV RNQIKHFAQK KLHLPPGKHK IVILDEADSM TAGAQQALRR TMELYSNSTR FAFACNQSNK IIEPLQSRCA I LRYSKLSD ...String:
MSKTLSLQLP WVEKYRPQVL SDIVGNKETI DRLQQIAKDG NMPHMIISGM PGIGKTTSVH CLAHELLGRS YADGVLELNA SDDRGIDVV RNQIKHFAQK KLHLPPGKHK IVILDEADSM TAGAQQALRR TMELYSNSTR FAFACNQSNK IIEPLQSRCA I LRYSKLSD EDVLKRLLQI IKLEDVKYTN DGLEAIIFTA EGDMRQAINN LQSTVAGHGL VNADNVFKIV DSPHPLIVKK ML LASNLED SIQILRTDLW KKGYSSIDIV TTSFRVTKNL AQVKESVRLE MIKEIGLTHM RILEGVGTYL QLASMLAKIH KLN NKA

UniProtKB: Replication factor C subunit 4

+
Macromolecule #3: Replication factor C subunit 3

MacromoleculeName: Replication factor C subunit 3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 37.841051 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSTSTEKRSK ENLPWVEKYR PETLDEVYGQ NEVITTVRKF VDEGKLPHLL FYGPPGTGKT STIVALAREI YGKNYSNMVL ELNASDDRG IDVVRNQIKD FASTRQIFSK GFKLIILDEA DAMTNAAQNA LRRVIERYTK NTRFCVLANY AHKLTPALLS R CTRFRFQP ...String:
MSTSTEKRSK ENLPWVEKYR PETLDEVYGQ NEVITTVRKF VDEGKLPHLL FYGPPGTGKT STIVALAREI YGKNYSNMVL ELNASDDRG IDVVRNQIKD FASTRQIFSK GFKLIILDEA DAMTNAAQNA LRRVIERYTK NTRFCVLANY AHKLTPALLS R CTRFRFQP LPQEAIERRI ANVLVHEKLK LSPNAEKALI ELSNGDMRRV LNVLQSCKAT LDNPDEDEIS DDVIYECCGA PR PSDLKAV LKSILEDDWG TAHYTLNKVR SAKGLALIDL IEGIVKILED YELQNEETRV HLLTKLADIE YSISKGGNDQ IQG SAVIGA IKASFENETV

UniProtKB: Replication factor C subunit 3

+
Macromolecule #4: Replication factor C subunit 2

MacromoleculeName: Replication factor C subunit 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 39.794473 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MFEGFGPNKK RKISKLAAEQ SLAQQPWVEK YRPKNLDEVT AQDHAVTVLK KTLKSANLPH MLFYGPPGTG KTSTILALTK ELYGPDLMK SRILELNASD ERGISIVREK VKNFARLTVS KPSKHDLENY PCPPYKIIIL DEADSMTADA QSALRRTMET Y SGVTRFCL ...String:
MFEGFGPNKK RKISKLAAEQ SLAQQPWVEK YRPKNLDEVT AQDHAVTVLK KTLKSANLPH MLFYGPPGTG KTSTILALTK ELYGPDLMK SRILELNASD ERGISIVREK VKNFARLTVS KPSKHDLENY PCPPYKIIIL DEADSMTADA QSALRRTMET Y SGVTRFCL ICNYVTRIID PLASRCSKFR FKALDASNAI DRLRFISEQE NVKCDDGVLE RILDISAGDL RRGITLLQSA SK GAQYLGD GKNITSTQVE ELAGVVPHDI LIEIVEKVKS GDFDEIKKYV NTFMKSGWSA ASVVNQLHEY YITNDNFDTN FKN QISWLL FTTDSRLNNG TNEHIQLLNL LVKISQL

UniProtKB: Replication factor C subunit 2

+
Macromolecule #5: Replication factor C subunit 5

MacromoleculeName: Replication factor C subunit 5 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 39.993582 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSLWVDKYRP KSLNALSHNE ELTNFLKSLS DQPRDLPHLL LYGPNGTGKK TRCMALLESI FGPGVYRLKI DVRQFVTASN RKLELNVVS SPYHLEITPS DMGNNDRIVI QELLKEVAQM EQVDFQDSKD GLAHRYKCVI INEANSLTKD AQAALRRTME K YSKNIRLI ...String:
MSLWVDKYRP KSLNALSHNE ELTNFLKSLS DQPRDLPHLL LYGPNGTGKK TRCMALLESI FGPGVYRLKI DVRQFVTASN RKLELNVVS SPYHLEITPS DMGNNDRIVI QELLKEVAQM EQVDFQDSKD GLAHRYKCVI INEANSLTKD AQAALRRTME K YSKNIRLI MVCDSMSPII APIKSRCLLI RCPAPSDSEI STILSDVVTN ERIQLETKDI LKRIAQASNG NLRVSLLMLE SM ALNNELA LKSSSPIIKP DWIIVIHKLT RKIVKERSVN SLIECRAVLY DLLAHCIPAN IILKELTFSL LDVETLNTTN KSS IIEYSS VFDERLSLGN KAIFHLEGFI AKVMCCLD

UniProtKB: Replication factor C subunit 5

+
Macromolecule #6: DNA damage checkpoint control protein MEC3

MacromoleculeName: DNA damage checkpoint control protein MEC3 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 53.207797 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MKLKLIVNGC EAPDDYKLLR TTINTVASLR KTAILRFNSE RLTIISTPKS SLNSSNNGTI LRGDTGQLWC TIPHDVFRLY TVISARELN TITMECNCDS LLSVFKRYDR VMNQGSSSNM TIKLQSMPEW NTNNGTLSGG TAGGVDTTSK PNPICALGIT F EEIVHTSG ...String:
MKLKLIVNGC EAPDDYKLLR TTINTVASLR KTAILRFNSE RLTIISTPKS SLNSSNNGTI LRGDTGQLWC TIPHDVFRLY TVISARELN TITMECNCDS LLSVFKRYDR VMNQGSSSNM TIKLQSMPEW NTNNGTLSGG TAGGVDTTSK PNPICALGIT F EEIVHTSG PNDAIVMNGG VDEHNGLPTT VGTGNLLASN KVIMHSFKVP VKLLFRAQDT RIQEPMINYI QLMMYKLPPI SG EFGSAFH GFIRRVERYS NVNHIHLMGV KKKEHGNEGD DVELKIIVNE LDWHLEICWN GPLDSVIQRQ EGLTDNPSQN QHI DTDGRQ EEGSLPIIEA DKPMSSLYTN TRDREMEENI RYDEDLLRIE DSSIADTRGN IYTADTSGDT EFNDISVMVE KAEQ ESSST HEVIIRCKDW KVCSKLYAAF EEVVLAISHD ESCVFHCSLD RGSLEDSEDV EKPRERGQII YYIARSKGL

UniProtKB: DNA damage checkpoint control protein MEC3

+
Macromolecule #7: DNA damage checkpoint control protein RAD17

MacromoleculeName: DNA damage checkpoint control protein RAD17 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 45.637527 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MRINSELANK FSASTVHLEH ITTALSCLTP FGSKDDVLIF IDADGLSFVR ENNHVIKIQL LLSRELFMSY SYRNETEDHM KLCVKINHI LDSVSVMNRN SDDIVECTLS YDGHGSPFVL IFEDSFISER VEYSTYLIKD FDTNGLELDR ERISFEAIIK G EALHSALK ...String:
MRINSELANK FSASTVHLEH ITTALSCLTP FGSKDDVLIF IDADGLSFVR ENNHVIKIQL LLSRELFMSY SYRNETEDHM KLCVKINHI LDSVSVMNRN SDDIVECTLS YDGHGSPFVL IFEDSFISER VEYSTYLIKD FDTNGLELDR ERISFEAIIK G EALHSALK DLKEIGCKEC YVYAKTEAND ENVFALISKS QLGFSKIKLP SNRSILEKLQ VFDGDSTTVI DGFAVIGFFD FT SFDKIRK STKIASKVLF RMDVHGVLSV NILSQTDDVI ITDTTRPSNN RPGSIRQLQL PKDYPGIVIE VCMLEKESID EAA QTEIEL LMETNELGNR NSFKKSTIRK RYGTDKGNET SNDNLLQLNG KKIKLPSEEE NNKNRESEDE ENHCKYPTKD IPIF F

UniProtKB: DNA damage checkpoint control protein RAD17

+
Macromolecule #8: DDC1 isoform 1

MacromoleculeName: DDC1 isoform 1 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 69.7875 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSFKATITES GKQNIWFRAI YVLSTIQDDI KITVTTNELI AWSMNETDTT LCQVRFQKSF FEEYEFKPHE IVFGENGVQV IEDTYGNSH KLYSFRVNGR HLTTISRKPD GDGIKSFTIA VNNTSTCPES LANRLIVVIE MDSLIVKEYC PQFQPIKYDP I IINLKYKR ...String:
MSFKATITES GKQNIWFRAI YVLSTIQDDI KITVTTNELI AWSMNETDTT LCQVRFQKSF FEEYEFKPHE IVFGENGVQV IEDTYGNSH KLYSFRVNGR HLTTISRKPD GDGIKSFTIA VNNTSTCPES LANRLIVVIE MDSLIVKEYC PQFQPIKYDP I IINLKYKR RFLDVFGTAA SDRNPQEPLD PKLLDVFTNT ERELTSALFN EEVESDIRKR NQLTAADEIN YICCNSTLLK NF LDNCNVN VTDEVKLEIN VHRLSITAFT KAVYGKNNDL LRNALSMSNT ISTLDLEHYC LFTTIEDEKQ DKRSHSKRRE HMK SIIFKL KDFKNFITIG PSWKTTQDGN DNISLWFCHP GDPILMQMQK PGVKLELVEV TDSNINDDIL EGKFIKTAIS GSKE EAGLK DNKESCESPL KSKTALKREN LPHSVAGTRN SPLKVSYLTP DNGSTVAKTY RNNTARKLFV EEQSQSTNYE QDKRF RQAS SVHMNMNREQ SFDIGTTHEV ACPRNESNSL KRSIADICNE TEDPTQQSTF AKRADTTVTW GKALPAADDE VSCSNI DRK GMLKKEKLKH MQGLLNSQND TSNHKKQDNK EMEDGLGLTQ VEKPRGIFD

UniProtKB: DDC1 isoform 1

+
Macromolecule #9: Template strand

MacromoleculeName: Template strand / type: dna / ID: 9 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 15.389855 KDa
SequenceString:
(DC)(DG)(DG)(DT)(DA)(DT)(DA)(DG)(DG)(DC) (DG)(DA)(DT)(DA)(DC)(DG)(DA)(DA)(DT)(DC) (DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DC)(DC)(DG)(DT)(DA)(DT)(DA)(DG)(DC) (DC) (DG)(DT)(DA)(DG)(DC)(DG)(DA)(DG) (DC)(DC)

+
Macromolecule #10: Primer strand 1

MacromoleculeName: Primer strand 1 / type: dna / ID: 10 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 6.464172 KDa
SequenceString:
(DG)(DG)(DC)(DT)(DC)(DG)(DC)(DT)(DA)(DC) (DG)(DG)(DC)(DT)(DA)(DT)(DA)(DC)(DG)(DG) (DA)

+
Macromolecule #11: Primer strand 2

MacromoleculeName: Primer strand 2 / type: dna / ID: 11 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 6.08494 KDa
SequenceString:
(DG)(DA)(DT)(DT)(DC)(DG)(DT)(DA)(DT)(DC) (DG)(DC)(DC)(DT)(DA)(DT)(DA)(DC)(DC)(DG)

+
Macromolecule #12: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER

MacromoleculeName: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / type: ligand / ID: 12 / Number of copies: 4 / Formula: AGS
Molecular weightTheoretical: 523.247 Da
Chemical component information

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

+
Macromolecule #13: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 13 / Number of copies: 4 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #14: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 14 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 64.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.9000000000000001 µm / Nominal defocus min: 1.3 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: NONE
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7sgz

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.94 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 347098
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

+
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