4JLX
Structure of porcine cyclic GMP-AMP synthase (cGAS)
Summary for 4JLX
| Entry DOI | 10.2210/pdb4jlx/pdb |
| Related | 4JLZ |
| Descriptor | Uncharacterized protein, ZINC ION, MALONATE ION, ... (6 entities in total) |
| Functional Keywords | dna binding protein |
| Biological source | Sus scrofa (pigs,swine,wild boar) |
| Total number of polymer chains | 1 |
| Total formula weight | 43324.26 |
| Authors | Civril, F.,Hopfner, K.P. (deposition date: 2013-03-13, release date: 2013-06-12, Last modification date: 2024-03-20) |
| Primary citation | Civril, F.,Deimling, T.,Mann, C.C.O.,Ablasser, A.,Moldt, M.,Witte, G.,Hornung, V.,Hopfner, K.P. Structural mechanism of cytosolic DNA sensing by cGAS Nature, 498:332-337, 2013 Cited by PubMed Abstract: Cytosolic DNA arising from intracellular bacterial or viral infections is a powerful pathogen-associated molecular pattern (PAMP) that leads to innate immune host defence by the production of type I interferon and inflammatory cytokines. Recognition of cytosolic DNA by the recently discovered cyclic-GMP-AMP (cGAMP) synthase (cGAS) induces the production of cGAMP to activate the stimulator of interferon genes (STING). Here we report the crystal structure of cGAS alone and in complex with DNA, ATP and GTP along with functional studies. Our results explain the broad DNA sensing specificity of cGAS, show how cGAS catalyses dinucleotide formation and indicate activation by a DNA-induced structural switch. cGAS possesses a remarkable structural similarity to the antiviral cytosolic double-stranded RNA sensor 2'-5'oligoadenylate synthase (OAS1), but contains a unique zinc thumb that recognizes B-form double-stranded DNA. Our results mechanistically unify dsRNA and dsDNA innate immune sensing by OAS1 and cGAS nucleotidyl transferases. PubMed: 23722159DOI: 10.1038/nature12305 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.004 Å) |
Structure validation
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