+
Open data
-
Basic information
| Entry | ![]() | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Focus refined map of E. coli clamp loader sub-complex Psi-Chi | ||||||||||||
Map data | focused map | ||||||||||||
Sample |
| ||||||||||||
Keywords | E. Coli / DNA replication / DNA damage repair / clamp loading complex / clamp beta / clamp loader DnaX-complex / REPLICATION | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 5.5 Å | ||||||||||||
Authors | Zheng F / Yao YN / Georgescu R / O'Donnell ME / Li H | ||||||||||||
| Funding support | United States, 3 items
| ||||||||||||
Citation | Journal: Mol Cell / Year: 2026Title: The E. coli DnaX clamp loader sharply bends DNA to load β-clamp at nicks and small gaps. Authors: Fengwei Zheng / Nina Y Yao / Roxana E Georgescu / Meinan Lyu / Michael E O'Donnell / Huilin Li / ![]() Abstract: DNA sliding clamps are essential for processive DNA synthesis in all domains of life and are loaded by ATP-dependent clamp loaders that recognize recessed 3' ends. How clamp loaders function at nicks ...DNA sliding clamps are essential for processive DNA synthesis in all domains of life and are loaded by ATP-dependent clamp loaders that recognize recessed 3' ends. How clamp loaders function at nicks and small single-stranded DNA (ssDNA) gaps-common DNA repair intermediates-remains unclear. Here, we show that the bacterial E. coli DnaX clamp loader uses a mechanism distinct from its eukaryotic counterpart. Whereas eukaryotic replication factor C (RFC) unwinds DNA at the recessed 3' end and stabilizes the 5'-dsDNA (double-stranded DNA) at a shoulder site, the bacterial DnaX-complex neither unwinds DNA nor stably binds the 5'-dsDNA in vitro. Instead, cryo-EM structures reveal that the β-clamp contains a conserved external DNA-binding site that bends gapped DNA by ∼150°, promoting insertion of 3'-dsDNA into the clamp. This DNA-bending mechanism enables efficient β-clamp loading at nicks and small gaps and reveals a distinct bacterial strategy likely important for DNA repair. | ||||||||||||
| History |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_71020.map.gz | 167.7 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-71020-v30.xml emd-71020.xml | 18.2 KB 18.2 KB | Display Display | EMDB header |
| Images | emd_71020.png | 9.2 KB | ||
| Filedesc metadata | emd-71020.cif.gz | 4.6 KB | ||
| Others | emd_71020_half_map_1.map.gz emd_71020_half_map_2.map.gz | 165.3 MB 165.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-71020 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-71020 | HTTPS FTP |
-Related structure data
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|
-
Map
| File | Download / File: emd_71020.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Annotation | focused map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.828 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Half map: half map A
| File | emd_71020_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Annotation | half map A | ||||||||||||
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: half map B
| File | emd_71020_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Annotation | half map B | ||||||||||||
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : E. coli clamp loading complex
| Entire | Name: E. coli clamp loading complex |
|---|---|
| Components |
|
-Supramolecule #1: E. coli clamp loading complex
| Supramolecule | Name: E. coli clamp loading complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#11 |
|---|
-Supramolecule #2: E. coli clamp loader sub-complex Psi-Chi
| Supramolecule | Name: E. coli clamp loader sub-complex Psi-Chi / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#7, #10 |
|---|---|
| Source (natural) | Organism: ![]() |
-Supramolecule #3: 10-nt gapped DNA substrate
| Supramolecule | Name: 10-nt gapped DNA substrate / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #8-#9, #11 |
|---|---|
| Source (natural) | Organism: DNA molecule (others) |
-Macromolecule #1: E. coli clamp loader sub-complex Psi-Chi
| Macromolecule | Name: E. coli clamp loader sub-complex Psi-Chi / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
|---|---|
| Sequence | String: SRRDWQLQQL GITQWSLRRP GALQGEIAIA IPAHVRLVMV ANDLPALTDP LVSDVLRALT VSPDQVLQLT PEKIAMLPQG SHCNSWRLG TDEPLSLEGA QVASPALTDL RANPTARAAL WQQICTYEHD FFPKNATFYL LDNDTTVDGL SAVEQLVCEI AAERWRSGKR ...String: SRRDWQLQQL GITQWSLRRP GALQGEIAIA IPAHVRLVMV ANDLPALTDP LVSDVLRALT VSPDQVLQLT PEKIAMLPQG SHCNSWRLG TDEPLSLEGA QVASPALTDL RANPTARAAL WQQICTYEHD FFPKNATFYL LDNDTTVDGL SAVEQLVCEI AAERWRSGKR VLIACEDEKQ AYRLDEALWA RPAESFVPHN LAGEGPRGGA PVE IAWPQK RSSSRRDILI SLRTSFADFA TAFTEVVDFV PYEDSLKQLA RERYKAYRVA GFNLNTATWK |
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Buffer | pH: 7.5 |
|---|---|
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 49.6 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
Movie
Controller
About Yorodumi




Keywords
Authors
United States, 3 items
Citation

Z (Sec.)
Y (Row.)
X (Col.)




































Processing
FIELD EMISSION GUN

