8JSJ

Crystal structure of an N-terminal cyclic nucleotide-binding domain of a PycTIR from Novosphingobium pentaromativorans

8JSJ の概要

• エントリーDOI: 10.2210/pdb8jsj/pdb
• 関連するPDBエントリー: 8JSF
• 分子名称: PycTIR (2 entities in total)
• 機能のキーワード: cump receptor, pycsar effector protein, signaling protein
• 由来する生物種: Novosphingobium pentaromativorans US6-1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34018.61

構造登録者

Wang, Y.-C.,Yang, C.-S.,Hou, M.-H.,Chen, Y. (登録日: 2023-06-20, 公開日: 2024-07-03, 最終更新日: 2024-07-17)

主引用文献

Hou, M.H.,Chen, C.J.,Yang, C.S.,Wang, Y.C.,Chen, Y.
Structural and functional characterization of cyclic pyrimidine-regulated anti-phage system.
Nat Commun, 15:5634-5634, 2024

PubMed Abstract: 3',5'-cyclic uridine monophosphate (cUMP) and 3',5'-cyclic cytidine monophosphate (cCMP) have been established as bacterial second messengers in the phage defense system, named pyrimidine cyclase system for anti-phage resistance (Pycsar). This system consists of a pyrimidine cyclase and a cyclic pyrimidine receptor protein. However, the molecular mechanism underlying cyclic pyrimidine synthesis and recognition remains unclear. Herein, we determine the crystal structures of a uridylate cyclase and a cytidylate cyclase, revealing the conserved residues for cUMP and cCMP production, respectively. In addition, a distinct zinc-finger motif of the uridylate cyclase is identified to confer substantial resistance against phage infections. Furthermore, structural characterization of cUMP receptor protein PycTIR provides clear picture of specific cUMP recognition and identifies a conserved N-terminal extension that mediates PycTIR oligomerization and activation. Overall, our results contribute to the understanding of cyclic pyrimidine-mediated bacterial defense.

PubMed: 38965224
DOI: 10.1038/s41467-024-49861-2

実験手法

X-RAY DIFFRACTION (2.858 Å)