8x51

Structure of DNA-bound GajA dimer (focused refinement)

spinqualitylabelsall models 8x51, resolution 2.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8x51 is a 4 chain structure with sequence from Bacillus cereus VD045 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.92Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Prokaryotes have evolved intricate innate immune systems against phage infection(1-7). Gabija is a highly widespread prokaryotic defence system that consists of two components, GajA and GajB(8). GajA functions as a DNA endonuclease that is inactive in the presence of ATP(9). Here, to explore how the Gabija system is activated for anti-phage defence, we report its cryo-electron microscopy structures in five states, including apo GajA, GajA in complex with DNA, GajA bound by ATP, apo GajA-GajB, and GajA-GajB in complex with ATP and Mg(2+). GajA is a rhombus-shaped tetramer with its ATPase domain clustered at the centre and the topoisomerase-primase (Toprim) domain located peripherally. ATP binding at the ATPase domain stabilizes the insertion region within the ATPase domain, keeping the Toprim domain in a closed state. Upon ATP depletion by phages, the Toprim domain opens to bind and cleave the DNA substrate. GajB, which docks on GajA, is activated by the cleaved DNA, ultimately leading to prokaryotic cell death. Our study presents a mechanistic landscape of Gabija activation. Structures and activation mechanism of the Gabija anti-phage system.,Li J, Cheng R, Wang Z, Yuan W, Xiao J, Zhao X, Du X, Xia S, Wang L, Zhu B, Wang L Nature. 2024 May;629(8011):467-473. doi: 10.1038/s41586-024-07270-x. Epub 2024 , Mar 12. PMID:38471529 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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