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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-14085 | ||||||||||||||||||
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| Title | 26S proteasome Rpt1-RK -Ubp6-UbVS complex in the s2 state | ||||||||||||||||||
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Keywords | proteasome / ubiquitin / Ubp6 / allostery / deubiquitination / MOTOR PROTEIN | ||||||||||||||||||
| Function / homology | Function and homology informationSAGA complex localization to transcription regulatory region / proteasome regulatory particle assembly / transcription export complex 2 / maintenance of DNA trinucleotide repeats / filamentous growth / proteasome-activating activity / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / proteasome core complex / Proteasome assembly ...SAGA complex localization to transcription regulatory region / proteasome regulatory particle assembly / transcription export complex 2 / maintenance of DNA trinucleotide repeats / filamentous growth / proteasome-activating activity / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / proteasome core complex / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / proteasomal ubiquitin-independent protein catabolic process / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / regulation of protein catabolic process / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / protein deubiquitination / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / Ub-specific processing proteases / mRNA export from nucleus / proteasome assembly / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / enzyme regulator activity / Neutrophil degranulation / protein folding chaperone / proteasome complex / double-strand break repair via homologous recombination / metallopeptidase activity / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity / endopeptidase activity / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / regulation of cell cycle / ubiquitin protein ligase binding / structural molecule activity / endoplasmic reticulum / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() Homo sapiens (human) | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 6.3 Å | ||||||||||||||||||
Authors | Hung KYS / Klumpe S / Eisele MR / Elsasser S / Geng TT / Cheng TC / Joshi T / Rudack T / Sakata E / Finley D | ||||||||||||||||||
| Funding support | Germany, 5 items
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Citation | Journal: Nat Commun / Year: 2022Title: Allosteric control of Ubp6 and the proteasome via a bidirectional switch. Authors: Ka Ying Sharon Hung / Sven Klumpe / Markus R Eisele / Suzanne Elsasser / Geng Tian / Shuangwu Sun / Jamie A Moroco / Tat Cheung Cheng / Tapan Joshi / Timo Seibel / Duco Van Dalen / Xin-Hua ...Authors: Ka Ying Sharon Hung / Sven Klumpe / Markus R Eisele / Suzanne Elsasser / Geng Tian / Shuangwu Sun / Jamie A Moroco / Tat Cheung Cheng / Tapan Joshi / Timo Seibel / Duco Van Dalen / Xin-Hua Feng / Ying Lu / Huib Ovaa / John R Engen / Byung-Hoon Lee / Till Rudack / Eri Sakata / Daniel Finley / ![]() Abstract: The proteasome recognizes ubiquitinated proteins and can also edit ubiquitin marks, allowing substrates to be rejected based on ubiquitin chain topology. In yeast, editing is mediated by ...The proteasome recognizes ubiquitinated proteins and can also edit ubiquitin marks, allowing substrates to be rejected based on ubiquitin chain topology. In yeast, editing is mediated by deubiquitinating enzyme Ubp6. The proteasome activates Ubp6, whereas Ubp6 inhibits the proteasome through deubiquitination and a noncatalytic effect. Here, we report cryo-EM structures of the proteasome bound to Ubp6, based on which we identify mutants in Ubp6 and proteasome subunit Rpt1 that abrogate Ubp6 activation. The Ubp6 mutations define a conserved region that we term the ILR element. The ILR is found within the BL1 loop, which obstructs the catalytic groove in free Ubp6. Rpt1-ILR interaction opens the groove by rearranging not only BL1 but also a previously undescribed network of three interconnected active-site-blocking loops. Ubp6 activation and noncatalytic proteasome inhibition are linked in that they are eliminated by the same mutations. Ubp6 and ubiquitin together drive proteasomes into a unique conformation associated with proteasome inhibition. Thus, a multicomponent allosteric switch exerts simultaneous control over both Ubp6 and the proteasome. | ||||||||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
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Downloads & links
-EMDB archive
| Map data | emd_14085.map.gz | 185 MB | EMDB map data format | |
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| Header (meta data) | emd-14085-v30.xml emd-14085.xml | 62.9 KB 62.9 KB | Display Display | EMDB header |
| Images | emd_14085.png | 110.7 KB | ||
| Filedesc metadata | emd-14085.cif.gz | 16.6 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-14085 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14085 | HTTPS FTP |
-Validation report
| Summary document | emd_14085_validation.pdf.gz | 514 KB | Display | EMDB validaton report |
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| Full document | emd_14085_full_validation.pdf.gz | 513.6 KB | Display | |
| Data in XML | emd_14085_validation.xml.gz | 7.4 KB | Display | |
| Data in CIF | emd_14085_validation.cif.gz | 8.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14085 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14085 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7qo6MC ![]() 7qo3C ![]() 7qo5C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_14085.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.38 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : 26S proteasome Rpt1-RK -Ubp6-UbVS complex in the s2 state
+Supramolecule #1: 26S proteasome Rpt1-RK -Ubp6-UbVS complex in the s2 state
+Macromolecule #1: BJ4_G0020160.mRNA.1.CDS.1
+Macromolecule #2: HLJ1_G0039880.mRNA.1.CDS.1
+Macromolecule #3: BJ4_G0021480.mRNA.1.CDS.1
+Macromolecule #4: HLJ1_G0048980.mRNA.1.CDS.1
+Macromolecule #5: EM14S01-3B_G0035190.mRNA.1.CDS.1
+Macromolecule #6: BJ4_G0043800.mRNA.1.CDS.1
+Macromolecule #7: Probable proteasome subunit alpha type-7
+Macromolecule #8: Proteasome subunit beta type-1
+Macromolecule #9: Proteasome endopeptidase complex
+Macromolecule #10: Proteasome endopeptidase complex
+Macromolecule #11: Proteasome subunit beta
+Macromolecule #12: Proteasome subunit beta type-5
+Macromolecule #13: HLJ1_G0013750.mRNA.1.CDS.1
+Macromolecule #14: Proteasome subunit beta type-7
+Macromolecule #15: 26S proteasome regulatory subunit RPN10
+Macromolecule #16: 26S proteasome regulatory subunit RPN11
+Macromolecule #17: EM14S01-3B_G0050020.mRNA.1.CDS.1
+Macromolecule #18: HLJ1_G0030700.mRNA.1.CDS.1
+Macromolecule #19: 26S proteasome complex subunit SEM1
+Macromolecule #20: 26S proteasome regulatory subunit RPN1
+Macromolecule #21: 26S proteasome regulatory subunit RPN2
+Macromolecule #22: 26S proteasome regulatory subunit RPN3
+Macromolecule #23: 26S proteasome regulatory subunit RPN5
+Macromolecule #24: 26S proteasome regulatory subunit RPN6
+Macromolecule #25: 26S proteasome regulatory subunit RPN7
+Macromolecule #26: 26S proteasome regulatory subunit RPN8
+Macromolecule #27: 26S proteasome regulatory subunit RPN9
+Macromolecule #28: 26S proteasome regulatory subunit 7 homolog
+Macromolecule #29: 26S proteasome regulatory subunit 4 homolog
+Macromolecule #30: 26S proteasome regulatory subunit 6B homolog
+Macromolecule #31: 26S proteasome subunit RPT4
+Macromolecule #32: 26S proteasome regulatory subunit 6A
+Macromolecule #33: 26S proteasome regulatory subunit 8 homolog
+Macromolecule #34: Ubiquitin carboxyl-terminal hydrolase
+Macromolecule #35: Polyubiquitin-B
+Macromolecule #36: ADENOSINE-5'-TRIPHOSPHATE
+Macromolecule #37: MAGNESIUM ION
+Macromolecule #38: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1.5 mg/mL |
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| Buffer | pH: 7.4 |
| Grid | Model: Quantifoil R2/1 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 35.0 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: 3.0 µm / Nominal defocus min: 1.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Germany, 5 items
Citation

UCSF Chimera
































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
























Processing
