Park Shin Hye Slim Down
Here, we present a crystallographic structure of the wild-type Synechococcus elongatus KaiB and a cryo-electron microscopy cryoEM structure of a KaiBC complex. Molecular dynamics simulations indicate higher mobility of the loop in the absence of the A-loop and mobility differences in other areas associated with phosphorylation activity between wild-type and mutant KaiCs. A maps to a loop loop that continues toward the phosphorylation sites.
Here, we present a crystallographic structure of the wild-type Synechococcus elongatus KaiB and a cryo-electron microscopy cryoEM structure of a KaiBC complex.
The crystal structure shows the expected dimer core structure and significant conformational variations of the KaiB C-terminal region, which is functionally important in maintaining rhythmicity. A KaiC mutation, RC, which has been shown to affect the affinity of KaiB for KaiC and lengthen the period in a bioluminescence rhythm assay, is found within the middle of the predicted KaiBC interface.
We demonstrate here that the AV KaiC mutant sheds light on the former mechanism.
It was previously reported that AV is less sensitive to dark pulse-induced phase resetting and has a reduced amplitude of the KaiC phosphorylation rhythm in vivo. The crystal structure shows the expected dimer core structure and significant conformational variations of the KaiB C-terminal region, which is functionally important in maintaining rhythmicity.
A KaiC mutation, RC, which has been shown to affect the affinity of KaiB for KaiC and lengthen the period in a bioluminescence rhythm assay, is found within the middle of the predicted KaiBC interface. We demonstrate here that the AV KaiC mutant sheds light on the former mechanism. It was previously reported that AV is less sensitive to dark pulse-induced phase resetting and has a reduced amplitude of the KaiC phosphorylation rhythm in vivo.
A maps to a loop loop that continues toward the phosphorylation sites.