Enzymes
| UniProtKB help_outline | 5 proteins |
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- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,280 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UTP Identifier CHEBI:46398 (Beilstein: 5204708) help_outline Charge -4 Formula C9H11N2O15P3 InChIKeyhelp_outline PGAVKCOVUIYSFO-XVFCMESISA-J SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 50 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3',3'-cUAMP Identifier CHEBI:143809 Charge -2 Formula C19H21N7O14P2 InChIKeyhelp_outline CYVLWDUVMGUTIY-KPKSGTNCSA-L SMILEShelp_outline [C@H]1(O[C@H]2[C@H]([C@H]1O)OP([O-])(OC[C@H]3O[C@@H](N4C=CC(NC4=O)=O)[C@@H]([C@@H]3OP([O-])(=O)OC2)O)=O)N5C=NC6=C5N=CN=C6N 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:60456 | RHEA:60457 | RHEA:60458 | RHEA:60459 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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cGLRs are a diverse family of pattern recognition receptors in innate immunity.
Li Y., Slavik K.M., Toyoda H.C., Morehouse B.R., de Oliveira Mann C.C., Elek A., Levy S., Wang Z., Mears K.S., Liu J., Kashin D., Guo X., Mass T., Sebe-Pedros A., Schwede F., Kranzusch P.J.
Cyclic GMP-AMP synthase (cGAS) is an enzyme in human cells that controls an immune response to cytosolic DNA. Upon binding DNA, cGAS synthesizes a nucleotide signal 2'3'-cGAMP that activates STING-dependent downstream immunity. Here, we discover that cGAS-like receptors (cGLRs) constitute a major ... >> More
Cyclic GMP-AMP synthase (cGAS) is an enzyme in human cells that controls an immune response to cytosolic DNA. Upon binding DNA, cGAS synthesizes a nucleotide signal 2'3'-cGAMP that activates STING-dependent downstream immunity. Here, we discover that cGAS-like receptors (cGLRs) constitute a major family of pattern recognition receptors in innate immunity. Building on recent analysis in Drosophila, we identify >3,000 cGLRs present in nearly all metazoan phyla. A forward biochemical screening of 150 animal cGLRs reveals a conserved mechanism of signaling including response to dsDNA and dsRNA ligands and synthesis of isomers of the nucleotide signals cGAMP, c-UMP-AMP, and c-di-AMP. Combining structural biology and in vivo analysis in coral and oyster animals, we explain how synthesis of distinct nucleotide signals enables cells to control discrete cGLR-STING signaling pathways. Our results reveal cGLRs as a widespread family of pattern recognition receptors and establish molecular rules that govern nucleotide signaling in animal immunity. << Less
Cell 186:3261-3276(2023) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.
Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R., Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S.Y., Mekalanos J.J., Kranzusch P.J.
Cyclic dinucleotides (CDNs) have central roles in bacterial homeostasis and virulence by acting as nucleotide second messengers. Bacterial CDNs also elicit immune responses during infection when they are detected by pattern-recognition receptors in animal cells. Here we perform a systematic bioche ... >> More
Cyclic dinucleotides (CDNs) have central roles in bacterial homeostasis and virulence by acting as nucleotide second messengers. Bacterial CDNs also elicit immune responses during infection when they are detected by pattern-recognition receptors in animal cells. Here we perform a systematic biochemical screen for bacterial signalling nucleotides and discover a large family of cGAS/DncV-like nucleotidyltransferases (CD-NTases) that use both purine and pyrimidine nucleotides to synthesize a diverse range of CDNs. A series of crystal structures establish CD-NTases as a structurally conserved family and reveal key contacts in the enzyme active-site lid that direct purine or pyrimidine selection. CD-NTase products are not restricted to CDNs and also include an unexpected class of cyclic trinucleotide compounds. Biochemical and cellular analyses of CD-NTase signalling nucleotides demonstrate that these cyclic di- and trinucleotides activate distinct host receptors and thus may modulate the interaction of both pathogens and commensal microbiota with their animal and plant hosts. << Less
Nature 567:194-199(2019) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.