Structural insights into cGAMP degradation by Ecto-nucleotide pyrophosphatase phosphodiesterase 1 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Kazuki Kato, Hiroshi Nishimasu, Daisuke Oikawa, Seiichi Hirano, Hisato Hirano, Go Kasuya, Ryuichiro Ishitani, Fuminori Tokunaga, Osamu Nureki

ABSTRACT

ENPP1 (Ecto-nucleotide pyrophosphatase phosphodiesterase 1), a type II transmembrane glycoprotein, hydrolyzes ATP to produce AMP and diphosphate, thereby inhibiting bone mineralization. A recent study showed that ENPP1 also preferentially hydrolyzes 2'3'-cGAMP (cyclic GMP-AMP) but not its linkage isomer 3'3'-cGAMP, and negatively regulates the cGAS-STING pathway in the innate immune system. Here, we present the high-resolution crystal structures of ENPP1 in complex with 3'3'-cGAMP and the reaction intermediate pA(3',5')pG. The structures revealed that the adenine and guanine bases of the dinucleotides are recognized by nucleotide- and guanine-pockets, respectively. Furthermore, the structures indicate that 2'3'-cGAMP, but not 3'3'-cGAMP, binds to the active site in a conformation suitable for catalysis, thereby explaining the specific degradation of 2'3'-cGAMP by ENPP1. Our findings provide insights into how ENPP1 hydrolyzes both ATP and cGAMP to participate in the two distinct biological processes. More... »

PAGES

4424

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-018-06922-7

DOI

http://dx.doi.org/10.1038/s41467-018-06922-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1107713153

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30356045


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