title: Convergent dynamics in the protease enzymatic superfamily.
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.
authors.affiliation: International School for Advanced Studies (SISSA) and INFM Democritos, Via Beirut 2-4, I-34014 Trieste, Italy.
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Carnevale
authors.forename: Simone
authors.initials: S
authors.lastname: Raugei
authors.forename: Cristian
authors.initials: C
authors.lastname: Micheletti
authors.forename: Paolo
authors.initials: P
authors.lastname: Carloni
mesh_terms: D019295:Computational Biology; D008958:Models, Molecular; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D010447:Peptide Hydrolases