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