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Structure paper

TitleCryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP.
Journal, issue, pagesNature, Vol. 567, Issue 7748, Page 389-393, Year 2019
Publish dateMar 6, 2019
AuthorsGuijun Shang / Conggang Zhang / Zhijian J Chen / Xiao-Chen Bai / Xuewu Zhang /
PubMed AbstractInfections 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.
External linksNature / PubMed:30842659 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 6.5 Å
Structure data

0502

6nt5

EMDB-0502, PDB-6nt5:
Cryo-EM structure of full-length human STING in the apo state
Method: EM (single particle) / Resolution: 4.1 Å

0503

6nt6

EMDB-0503, PDB-6nt6:
Cryo-EM structure of full-length chicken STING in the apo state
Method: EM (single particle) / Resolution: 4.0 Å

0504

6nt7

EMDB-0504, PDB-6nt7:
Cryo-EM structure of full-length chicken STING in the cGAMP-bound dimeric state
Method: EM (single particle) / Resolution: 4.0 Å

0505

6nt8

EMDB-0505, PDB-6nt8:
Cryo-EM structure of full-length chicken STING in the cGAMP-bound tetrameric state
Method: EM (single particle) / Resolution: 6.5 Å

Chemicals

ChemComp-1SY:
cGAMP / Cyclic guanosine monophosphate–adenosine monophosphate

Source
  • homo sapiens (human)
  • gallus gallus (chicken)
KeywordsIMMUNE SYSTEM / ER / membrane / adaptor

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