|Entry||Database: EMDB / ID: EMD-0503|
|Title||Cryo-EM structure of full-length chicken STING in the apo state|
|Sample||full-length chicken STING:|
Stimulator of interferon genes protein
|Function / homology|
Function and homology information
integral component of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane / interferon-beta production / cyclic-GMP-AMP binding / reticulophagy / cyclic-di-GMP binding / cellular response to interferon-beta / autophagosome membrane / cellular response to exogenous dsRNA / activation of innate immune response / positive regulation of defense response to virus by host ...integral component of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane / interferon-beta production / cyclic-GMP-AMP binding / reticulophagy / cyclic-di-GMP binding / cellular response to interferon-beta / autophagosome membrane / cellular response to exogenous dsRNA / activation of innate immune response / positive regulation of defense response to virus by host / integral component of endoplasmic reticulum membrane / autophagosome assembly / positive regulation of macroautophagy / autophagosome / positive regulation of type I interferon production / peroxisome / protein complex oligomerization / regulation of inflammatory response / defense response to virus / positive regulation of DNA-binding transcription factor activity / mitochondrial outer membrane / positive regulation of protein binding / endosome / transcription factor binding / endoplasmic reticulum membrane / ubiquitin protein ligase binding / innate immune response / protein kinase binding / Golgi apparatus / perinuclear region of cytoplasm / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / nucleoplasm / cytosol / cytoplasm
Stimulator of interferon genes protein, C-terminal domain superfamily / Stimulator of interferon genes protein, C-terminal / Stimulator of interferon genes protein
Stimulator of interferon genes protein / Stimulator of interferon genes protein
|Biological species||Gallus gallus (chicken)|
|Method||single particle reconstruction / cryo EM / Resolution: 4 Å|
|Authors||Shang G / Zhang C / Chen ZJ / Bai X / Zhang X|
|Funding support|| United States, 6 items |
|Citation||Journal: Nature / Year: 2019|
Title: Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP.
Authors: Guijun Shang / Conggang Zhang / Zhijian J Chen / Xiao-Chen Bai / Xuewu Zhang /
Abstract: Infections by pathogens that contain DNA trigger the production of type-I interferons and inflammatory cytokines through cyclic GMP-AMP synthase, which produces 2'3'-cyclic GMP-AMP (cGAMP) that binds ...Infections by pathogens that contain DNA trigger the production of type-I interferons and inflammatory cytokines through cyclic GMP-AMP synthase, which produces 2'3'-cyclic GMP-AMP (cGAMP) that binds to and activates stimulator of interferon genes (STING; also known as TMEM173, MITA, ERIS and MPYS). STING is an endoplasmic-reticulum membrane protein that contains four transmembrane helices followed by a cytoplasmic ligand-binding and signalling domain. The cytoplasmic domain of STING forms a dimer, which undergoes a conformational change upon binding to cGAMP. However, it remains unclear how this conformational change leads to STING activation. Here we present cryo-electron microscopy structures of full-length STING from human and chicken in the inactive dimeric state (about 80 kDa in size), as well as cGAMP-bound chicken STING in both the dimeric and tetrameric states. The structures show that the transmembrane and cytoplasmic regions interact to form an integrated, domain-swapped dimeric assembly. Closure of the ligand-binding domain, induced by cGAMP, leads to a 180° rotation of the ligand-binding domain relative to the transmembrane domain. This rotation is coupled to a conformational change in a loop on the side of the ligand-binding-domain dimer, which leads to the formation of the STING tetramer and higher-order oligomers through side-by-side packing. This model of STING oligomerization and activation is supported by our structure-based mutational analyses.
|Validation Report||PDB-ID: 6nt6|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_0503.map.gz / Format: CCP4 / Size: 18.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.84 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire full-length chicken STING
|Entire||Name: full-length chicken STING / Number of components: 2|
-Component #1: protein, full-length chicken STING
|Protein||Name: full-length chicken STING / Recombinant expression: No|
|Source||Species: Gallus gallus (chicken)|
|Source (engineered)||Expression System: Homo sapiens (human) / Cell of expression system: HEK293 GnTI-|
-Component #2: protein, Stimulator of interferon genes protein
|Protein||Name: Stimulator of interferon genes protein / Number of Copies: 2 / Recombinant expression: No|
|Mass||Theoretical: 44.20707 kDa|
|Source||Species: Gallus gallus (chicken)|
|Source (engineered)||Expression System: Homo sapiens (human)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Specimen conc.: 4.5 mg/mL / pH: 8|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 40 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD / Energy filter: GIF Quantum LS|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C2 (2 fold cyclic) / Number of projections: 164337|
|3D reconstruction||Software: RELION / Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF|
|FSC plot (resolution estimation)|
-Atomic model buiding
|Modeling #1||Refinement space: REAL|
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