9UXL

type II Lamassu, LmuACB from Vibrio cholerae O1 El

Summary for 9UXL

• Entry DOI: 10.2210/pdb9uxl/pdb
• EMDB information: 64586
• Descriptor: DUF3732 domain-containing protein, Lamassu C, ABC-three component systems C-terminal domain-containing protein (3 entities in total)
• Functional Keywords: endonuclease; structural maintenance of chromosomes (smc) proteins; dna binding protein, dna binding protein
• Biological source: Vibrio cholerae; More
• Total number of polymer chains: 4
• Total formula weight: 213808.78

Authors

Zhao, X.,Li, M.,Li, S.,Feng, Y.,Zhang, K. (deposition date: 2025-05-14, release date: 2026-03-25)

Primary citation

Li, M.,Zhao, X.,Zhao, X.,Li, D.,Xiong, W.,Gao, Z.,Huang, L.,An, L.,Gao, Y.,Li, S.,Feng, Y.,Zhang, K.,Zhang, Y.
Structural insights into type-I and type-II Lamassu antiphage systems.
Nat.Chem.Biol., 2026

PubMed Abstract: Bacteria have developed a variety of immune systems to combat phage infections. The Lamassu system is a prokaryotic immune system with a core conserved structural maintenance of chromosomes (SMC) superfamily protein LmuB and diverse effectors named LmuA, whose mechanism remains unclear. Here we present a series of cryo-electron microscopy structures of the type-I Lamassu complex from Bacillus cellulasensis and the type-II Lamassu complex from Vibrio cholerae, both in apo and dsDNA-bound states, revealing an unexpected stoichiometry and topological architecture distinct from canonical SMC complexes. Combined structural and biochemical analyses show how the nuclease effector LmuA is sequestered in an inactive monomeric form within the Lamassu complex and, upon sensing foreign DNA ends, dissociates and assembles into an active tetramer capable of DNA cleavage. Our findings elucidate the mechanism by which Lamassu systems detect viral replication and implement antiphage defense, highlighting the roles of SMC proteins in prokaryotic immunity.

PubMed: 41482579
DOI: 10.1038/s41589-025-02102-z

Experimental method

ELECTRON MICROSCOPY (4.07 Å)