Conformational Studies Suggest That the Double Stranded β Helix Scaffold Provides an Optimal Balance Between Protein Stability and Function

Title: Conformational Studies Suggest That the Double Stranded β Helix Scaffold Provides an Optimal Balance Between Protein Stability and Function

Volume: 15 Issue: 3

Author(s): B. Gopal, M. Rajavel and Neema N. Kulkarni

Affiliation:

Keywords: Double stranded beta helix, Cupin, Quercetinase, Conformational stability, Fragment complementation, Oligomerization

Abstract: 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.

Cite this article as:

Gopal B., Rajavel M. and Kulkarni N. Neema, Conformational Studies Suggest That the Double Stranded β Helix Scaffold Provides an Optimal Balance Between Protein Stability and Function, Protein & Peptide Letters 2008; 15 (3) . https://dx.doi.org/10.2174/092986608783744289