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A structure based suppression strategy permits the inactive variant Flp(W330A) to be rescued by a second site mutation A339M.
Applying live cell imaging, we for the first time show that pyroptosomes of enzymatically inactive variant caspase-1 spread during cell division.
In the inactive variant, a third class of N-terminal conformation is observed, which arises from a conformational change in the position of F17.
Substitution of Trp164 by His also resulted in an inactive variant, indicating that an indole side-chain is required for activity.
We present the structures of Escherichia coli ClpP to 1.9 Å and an inactive variant that provide some clues for how this might be achieved.
Here we aimed to investigate whether an enzymatically inactive variant caspase-1 (p.C284A) leads to the alteration of speck formation and pyroptosis, a caspase-1 dependent proinflammatory cell death.
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Inactive variants were defined as variants which showed no detectable activity in buffer.
Therefore, the number of inactive variants was the same for all four organic solvents.
Column "×" shows that the number of inactive variants resulted from amino acid substitutions.
The number of inactive variants was the same for all organic solvents.
These libraries, however, contain mostly inactive variants, and the very low frequency of improved variants can only be isolated by high-throughput screening.
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