Convergent dynamics in the protease enzymatic superfamily
Vincenzo Carnevale, Simone Raugei, Cristian Micheletti, Paolo Carloni
Abstract
Proteases regulate various aspects of the life cycle in all organisms by cleaving specific peptide bonds. Their action is so central for biochemical processes that at least 2% of any known genome encodes for proteolytic enzymes. Here we show that selected proteases pairs, despite differences in oligomeric state, catalytic residues and fold, share a common structural organization of functionally relevant regions which are further shown to undergo similar concerted movements. The structural and dynamical similarities found pervasively across evolutionarily distant clans point to common mechanisms for peptide hydrolysis.
Create a lesson
Related papers
A meta-algorithm for ab initio reconstruction of complex mixtures in cryo-EM
Alkin Kaz, Arda Kaz, Ellen D. Zhong
PHASE: encoding global protein ensembles with local Hamiltonians and all-atom backmapping
Daniele Angioletti, Marco Nobile, Matteo Carli et al.
Analysis of correlations of dwell-times of adjacent kinetic states in the activity of the cold and menthol receptor TRPM8
Ogloblya O. V., Moroz O. F., Zholos A.
Multitask Bayesian Neural Networks for Multiparameter Protein Engineering
Fabio Herrera-Rocha, David Medina-Ortiz, Desiree Wyrzykala et al.
Recovering protein conformations from single-particle cryo-EM data via indirect shape matching gradient flows
Erik Jansson, Jonathan Krook, Ozan Öktem et al.
Is Retrieval All You Need? Assessment and Emergence of Novelty in Protein Structure Generation
Tongyue Xu, Yijie Zhang, Mutian He et al.