8BSB

Vc1313-LBD bound to D-lysine

Summary for 8BSB

• Entry DOI: 10.2210/pdb8bsb/pdb
• Related: 8BSA
• Descriptor: Methyl-accepting chemotaxis protein, D-LYSINE (3 entities in total)
• Functional Keywords: ligand binding domain, membrane protein, methyl-accepting chemotaxis protein, chemotaxis
• Biological source: Vibrio cholerae (Vibrio cholerae serotype O1)
• Total number of polymer chains: 2
• Total formula weight: 40421.09

Authors

ter Beek, J.,Berntsson, R.P.-A. (deposition date: 2022-11-24, release date: 2023-06-07, Last modification date: 2024-05-01)

Primary citation

Irazoki, O.,Ter Beek, J.,Alvarez, L.,Mateus, A.,Colin, R.,Typas, A.,Savitski, M.M.,Sourjik, V.,Berntsson, R.P.,Cava, F.
D-amino acids signal a stress-dependent run-away response in Vibrio cholerae.
Nat Microbiol, 8:1549-1560, 2023

PubMed Abstract: To explore favourable niches while avoiding threats, many bacteria use a chemotaxis navigation system. Despite decades of studies on chemotaxis, most signals and sensory proteins are still unknown. Many bacterial species release D-amino acids to the environment; however, their function remains largely unrecognized. Here we reveal that D-arginine and D-lysine are chemotactic repellent signals for the cholera pathogen Vibrio cholerae. These D-amino acids are sensed by a single chemoreceptor MCP co-transcribed with the racemase enzyme that synthesizes them under the control of the stress-response sigma factor RpoS. Structural characterization of this chemoreceptor bound to either D-arginine or D-lysine allowed us to pinpoint the residues defining its specificity. Interestingly, the specificity for these D-amino acids appears to be restricted to those MCP orthologues transcriptionally linked to the racemase. Our results suggest that D-amino acids can shape the biodiversity and structure of complex microbial communities under adverse conditions.

PubMed: 37365341
DOI: 10.1038/s41564-023-01419-6

Experimental method

X-RAY DIFFRACTION (1.9 Å)