ArticleFrontiers in microbiology2025
Phosphorylation-driven conformational switching of the ArnA-ArnB complex involved in archaeal motility regulation.
Article in Frontiers in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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13 authors.
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Abstract
ArnA and ArnB serve as regulators within the Sulfolobus archaellum regulatory network by modulating the archaellum components ArlB and ArlX, which are essential for swimming motility. Together, they form a dynamic complex that, depending on nutrient availability, exists in either a loose, unphosphorylated or a tight, phosphorylated state. This transition is directed by phosphorylation via the kinase ArnC. To investigate this transition, we determined the cocrystal structure of the ArnA/ArnB complex, revealing that the zinc finger domain of ArnA interacts with both the β-sandwich and the C-terminal domains of ArnB. HDX data support the phosphorylation-dependent transition from a loose to a tight ArnAB complex driven by sequential phosphorylation of ArnB. This modification exposes the interaction surface of the C-terminal domain of ArnB, which then binds to the forkhead-associated domain of ArnA. Upon starvation of deletion strains of
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