6VM5

Structure of Moraxella osloensis Cap4 SAVED/CARF-domain containing receptor

6VM5 の概要

• エントリーDOI: 10.2210/pdb6vm5/pdb
• 分子名称: SAVED domain-containing protein, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: nuclease, duf4297, saved, carf, phage immunity, hydrolase
• 由来する生物種: Moraxella osloensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52638.49

構造登録者

Lowey, B.,Whiteley, A.T.,Keszei, A.F.A.,Morehouse, B.R.,Antine, S.P.,Cabrera, V.,Schwede, F.,Mekalanos, J.J.,Shao, S.,Lee, A.S.Y.,Kranzusch, P.J. (登録日: 2020-01-27, 公開日: 2020-06-17, 最終更新日: 2024-04-03)

主引用文献

Lowey, B.,Whiteley, A.T.,Keszei, A.F.A.,Morehouse, B.R.,Mathews, I.T.,Antine, S.P.,Cabrera, V.J.,Kashin, D.,Niemann, P.,Jain, M.,Schwede, F.,Mekalanos, J.J.,Shao, S.,Lee, A.S.Y.,Kranzusch, P.J.
CBASS Immunity Uses CARF-Related Effectors to Sense 3'-5'- and 2'-5'-Linked Cyclic Oligonucleotide Signals and Protect Bacteria from Phage Infection.
Cell, 182:38-, 2020

PubMed Abstract: cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzymes are immune sensors that synthesize nucleotide second messengers and initiate antiviral responses in bacterial and animal cells. Here, we discover Enterobacter cloacae CD-NTase-associated protein 4 (Cap4) as a founding member of a diverse family of >2,000 bacterial receptors that respond to CD-NTase signals. Structures of Cap4 reveal a promiscuous DNA endonuclease domain activated through ligand-induced oligomerization. Oligonucleotide recognition occurs through an appended SAVED domain that is an unexpected fusion of two CRISPR-associated Rossman fold (CARF) subunits co-opted from type III CRISPR immunity. Like a lock and key, SAVED effectors exquisitely discriminate 2'-5'- and 3'-5'-linked bacterial cyclic oligonucleotide signals and enable specific recognition of at least 180 potential nucleotide second messenger species. Our results reveal SAVED CARF family proteins as major nucleotide second messenger receptors in CBASS and CRISPR immune defense and extend the importance of linkage specificity beyond mammalian cGAS-STING signaling.

PubMed: 32544385
DOI: 10.1016/j.cell.2020.05.019

実験手法

X-RAY DIFFRACTION (2.35 Å)