Version 4 2021-02-11, 20:06Version 4 2021-02-11, 20:06
Version 3 2021-02-11, 11:48Version 3 2021-02-11, 11:48
Version 2 2021-01-29, 07:34Version 2 2021-01-29, 07:34
Version 1 2021-01-28, 13:19Version 1 2021-01-28, 13:19
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posted on 2021-02-11, 20:06authored byJ. VreedeJ. Vreede, Stanley Brul, Peter Setlow, Sophie Blinker
Bacillussubtilis forms dormant spores upon nutrient depletion. Germinant receptors (GRs) in spore’s inner membrane respond to ligands such as L-alanine, and trigger spore germination. In B. subtilis spores, GerA is the major GR, and has three subunits, GerAA, GerAB, and GerAC. L-Alanine activation of GerA requires all three subunits, but which binds L-alanine is unknown. To date, how GRs trigger germination is unknown, in particular due to lack of detailed structural information about B subunits. Using homology modelling with molecular dynamics (MD) simulations, we present structural predictions for the integral membrane protein GerAB. These predictions indicate that GerAB is an alpha-helical transmembrane protein containing a water channel. The MD simulations with free L-alanine show that alanine binds transiently to specific sites on GerAB. These results provide a starting point for unraveling the mechanism of L-alanine mediated signaling by GerAB, which may facilitate early events in spore germination.