|Entry||Database: EMDB / ID: EMD-2651|
|Title||Cryo-EM structure of human APC/C-Cdh1-Hsl1 complex at 7.4 A resolution|
|Sample||Recombinant human APC/C-Cdh1-Hsl1 ternary complex:|
|Keywords||Cullin-RING E3 ligase / Ubiquitination|
|Biological species||Homo sapiens (human)|
|Method||single particle reconstruction / cryo EM / Resolution: 7.4 Å|
|Authors||Chang LF / Zhang Z / Yang J / McLaughlin S / Barford D|
|Citation||Journal: Nature / Year: 2014|
Title: Molecular architecture and mechanism of the anaphase-promoting complex.
Authors: Lei-Fu Chang / Ziguo Zhang / Jing Yang / Stephen H McLaughlin / David Barford /
Abstract: The ubiquitination of cell cycle regulatory proteins by the anaphase-promoting complex/cyclosome (APC/C) controls sister chromatid segregation, cytokinesis and the establishment of the G1 phase of ...The ubiquitination of cell cycle regulatory proteins by the anaphase-promoting complex/cyclosome (APC/C) controls sister chromatid segregation, cytokinesis and the establishment of the G1 phase of the cell cycle. The APC/C is an unusually large multimeric cullin-RING ligase. Its activity is strictly dependent on regulatory coactivator subunits that promote APC/C-substrate interactions and stimulate its catalytic reaction. Because the structures of many APC/C subunits and their organization within the assembly are unknown, the molecular basis for these processes is poorly understood. Here, from a cryo-electron microscopy reconstruction of a human APC/C-coactivator-substrate complex at 7.4 Å resolution, we have determined the complete secondary structural architecture of the complex. With this information we identified protein folds for structurally uncharacterized subunits, and the definitive location of all 20 APC/C subunits within the 1.2 MDa assembly. Comparison with apo APC/C shows that the coactivator promotes a profound allosteric transition involving displacement of the cullin-RING catalytic subunits relative to the degron-recognition module of coactivator and APC10. This transition is accompanied by increased flexibility of the cullin-RING subunits and enhanced affinity for UBCH10-ubiquitin, changes which may contribute to coactivator-mediated stimulation of APC/C E3 ligase activity.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_2651.map.gz / Format: CCP4 / Size: 15.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 2.36 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Recombinant human APC/C-Cdh1-Hsl1 ternary complex
|Entire||Name: Recombinant human APC/C-Cdh1-Hsl1 ternary complex / Details: The sample was monodisperse / Number of components: 16|
|Mass||Theoretical: 1.2 MDa / Experimental: 1.2 MDa|
-Component #1: protein, Anaphase-promoting complex
|Protein||Name: Anaphase-promoting complex / a.k.a: CyclosomeAnaphase-promoting complex / Recombinant expression: Yes|
|Mass||Theoretical: 1.2 MDa / Experimental: 1.2 MDa|
|Source||Species: Homo sapiens (human)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.2 mg/mL|
|Vitrification||Instrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 100 %|
-Electron microscopy imaging
Model: Tecnai F20 / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI F20 / Date: Dec 12, 2012|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 25 e/Å2 / Illumination mode: OTHER|
|Lens||Imaging mode: BRIGHT FIELD / Defocus: 1500 - 4000 nm|
|Specimen Holder||Holder: Gatan 626 cryo-holder / Model: GATAN LIQUID NITROGEN|
|Camera||Detector: TVIPS TEMCAM-F415 (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 119386|
|3D reconstruction||Software: Relion / Resolution: 7.4 Å / Resolution method: FSC 0.143, gold-standard|
-Atomic model buiding
|Modeling #1||Refinement protocol: flexible / Refinement space: REAL|
Input PDB model: 1XPI
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