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PDB ID: 4K9A

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Ligands
Code Name Style Show Link
5GP Guanosine-5'-monophosphate PoSSuM
AMP Adenosine monophosphate PoSSuM
PO4 Phosphate ion PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 4K9A   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/DNA
Title : Structure of Ternary Complex of cGAS with dsDNA and Bound 5 -pG(2 ,5 )pA
Release Data : 2013-05-15
Compound :
mol_id molecule chains synonym
1 Cyclic GMP-AMP synthase A cGAMP synthase, cGAS, m-cGAS, Mab-21 domain-containing protein 1
ec: 2.7.7.-
fragment: C-TERMINAL DOMAIN, UNP residues 147-507
mol_id molecule chains
2 DNA-F D
mol_id molecule chains
3 DNA-R E
Source :
mol_id organism_scientific organism_common expression_system
1 Mus musculus  (taxid:10090) Mouse Escherichia coli  (taxid:562)
gene: Mb21d1
mol_id organism_scientific
2
synthetic: yes
other_details: This sequence was synthesized by regular protocol
mol_id organism_scientific
3
synthetic: yes
other_details: This sequence was synthesized by regular protocol
Authors : Gao, P., Wu, Y., Patel, D.J.
Keywords : nucleotidyltransferase fold, TRANSFERASE-DNA complex
Exp. method : X-RAY DIFFRACTION ( 2.264 Å )
Citation :

Cyclic [G(2',5')pA(3',5')p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase.

Gao, P.,Ascano, M.,Wu, Y.  et al.
(2013)  Cell(Cambridge,Mass.)  153 : 1094 - 1107

PubMed: 23647843
DOI: 10.1016/j.cell.2013.04.046

Reaction

Chain : A
UniProt : Q8C6L5 (CGAS_MOUSE)
Reaction: EC: Evidence:
Physiological Direction:
GTP + ATP = 2',3'-cGAMP + 2 diphosphate 2.7.7.86 PubMed:23647843, PubMed:28963528, PubMed:29976794, PubMed:30007416, PubMed:32814054
left-to-right PubMed:23258413
GTP + ATP = pppGp(2'-5')A + diphosphate - PubMed:23647843, PubMed:28963528, PubMed:29976794, PubMed:30007416, PubMed:32814054
left-to-right PubMed:23258413
pppGp(2'-5')A = 2',3'-cGAMP + diphosphate - PubMed:23647843, PubMed:28963528, PubMed:29976794, PubMed:30007416, PubMed:32814054
left-to-right PubMed:23258413
Cofactor: Evidence: Note:
Mn(2+) ECO:0000269 | PubMed:23647843
ECO:0000269 | PubMed:23647843
ECO:0000269 | PubMed:32814054
Binds 1 Mg(2+) per subunit (PubMed:23647843). Is also active with Mn(2+) (PubMed:23647843, PubMed:32814054). Mn(2+)-activated enzyme forms an inverted pppGp(2'-5')A intermediate, suggesting a non- canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over (PubMed:32814054). Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues (PubMed:32814054).
Zn(2+) ECO:0000269 | PubMed:29976794
ECO:0000269 | PubMed:32814054
ECO:0000269 | PubMed:32911480
ECO:0000269 | PubMed:32911481
ECO:0000269 | PubMed:32913000
Undergoes a liquid-like phase transition after binding to DNA, which is dependent on zinc.