The abstract is read at the publisher; the summary is JClub's.
In Bacillus subtilis, CdaR’s extracellular YbbR domains undergo a reversible conformational switch between pH 4.5 and 5.5, centered on a hinge between domains 1 and 2.
- Why it matters: Acidic host environments below pH 5 require Gram-positive bacteria to sense extracellular pH to adapt, but how CdaR detects acid and links it to c-di-AMP signaling was unclear.
- What they did: The study used SEC-MALS, mass photometry, circular dichroism, fluorescence assays, crystallography, molecular dynamics, and solution NMR to map a pH-dependent hinge transition requiring at least two tandem YbbR domains.
- The result: Mutating a conserved aspartate abolishes the conformational switch in vitro and accelerates low-pH adaptation in vivo, defining a structural mechanism that couples extracellular acidification to intracellular c-di-AMP signaling.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.