7LJL

Structure of the Enterobacter cloacae CD-NTase CdnD in complex with ATP

7LJL の概要

• エントリーDOI: 10.2210/pdb7ljl/pdb
• 分子名称: Cyclic AMP-AMP-GMP synthase, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: cd-ntase, cbass, transferase, trinucleotide
• 由来する生物種: Enterobacter cloacae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89384.73

構造登録者

Govande, A.,Lowey, B.,Eaglesham, J.B.,Whiteley, A.W.,Kranzusch, P.J. (登録日: 2021-01-29, 公開日: 2021-06-02, 最終更新日: 2024-04-03)

主引用文献

Govande, A.A.,Duncan-Lowey, B.,Eaglesham, J.B.,Whiteley, A.T.,Kranzusch, P.J.
Molecular basis of CD-NTase nucleotide selection in CBASS anti-phage defense.
Cell Rep, 35:109206-109206, 2021

PubMed Abstract: cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzymes are signaling proteins that initiate antiviral immunity in animal cells and cyclic-oligonucleotide-based anti-phage signaling system (CBASS) phage defense in bacteria. Upon phage recognition, bacterial CD-NTases catalyze synthesis of cyclic-oligonucleotide signals, which activate downstream effectors and execute cell death. How CD-NTases control nucleotide selection to specifically induce defense remains poorly defined. Here, we combine structural and nucleotide-analog interference-mapping approaches to identify molecular rules controlling CD-NTase specificity. Structures of the cyclic trinucleotide synthase Enterobacter cloacae CdnD reveal coordinating nucleotide interactions and a possible role for inverted nucleobase positioning during product synthesis. We demonstrate that correct nucleotide selection in the CD-NTase donor pocket results in the formation of a thermostable-protein-nucleotide complex, and we extend our analysis to establish specific patterns governing selectivity for each of the major bacterial CD-NTase clades A-H. Our results explain CD-NTase specificity and enable predictions of nucleotide second-messenger signals within diverse antiviral systems.

PubMed: 34077735
DOI: 10.1016/j.celrep.2021.109206

実験手法

X-RAY DIFFRACTION (1.45 Å)