TL;DR
The results suggest that the 52 knot in UCH-L1 is not a passive topological feature but a functional element that constrains unfolding dynamics and contributes to substrate binding efficiency.
Topologically knotted proteins are emerging as functional elements of the proteome rather than structural curiosities. Among the recurring protein knot types, the 31 trefoil, 52 Gordian and 71 septoil knots provide useful models for understanding how topology may reshape catalysis, substrate recognition, folding and me...
Together, these results establish recurrent catalytic-state change and physicochemical remodeling of the ancestral HEPN cleft, whether such remodeling corresponds to altered binding, regulation, or another molecular function remains a hypothesis requiring experimental testing.
An ensemble-based model in which pre-existing conformational organization shapes how the protein responds to the matched mutations is supported and stability-engineering mutations should be evaluated in the context of the parent ensemble is argued.
A highly conserved BECN1 domain located between previously characterized BH3 and coiled-coil domains is delineated and its structure and role in autophagy is elucidated.
Microtubule nucleation by γ-tubulin ring complexes (γ-TuRCs) must be spatiotemporally controlled to avoid major cell division errors. γ-TuRCs are activated by the centrosome-specific binding of a highly conserved centrosomin motif 1 (CM1) domain, but how binding is prevented in the cytosol remains unclear. We provide t...
Knotted proteins can present a distinct topological and mechanical challenge to the AAA+ cellular degradation machineries, determined by the relative size of the knot and the pore dimensions of these enzymes. In this study, we investigated the degradation mechanism of knotted proteins of different topological complexit...
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