Conformational studies suggest that the double stranded beta helix scaffold provides an optimal balance between protein stability and function.
Proteins with the double stranded beta-helix (DSBH, also known as cupin) fold perform a diverse range of functions. In this study, Bacillus subtilis quercetinase was used as a model system to understand the conformational determinants of functional diversity within the cupin fold. Controlled proteolysis experiments revealed that this enzyme is active, thermo-stable and maintains its quaternary arrangement even after substantial (ca 33 %) cleavage of the protein. The results presented in this manuscript thus show that the DSBH scaffold offers a novel balance between protein stability and function by locating the active site and substrate recognition features in the most stable region of the protein.
Rajavel
M
M
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
Kulkarni
Neema N
NN
Gopal
B
B
D001412:Bacillus subtilis / Q000201:enzymology; D001665:Binding Sites; D049308:Dioxygenases / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D049308:Dioxygenases; C003281:quercetin 2,3-dioxygenase