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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 15, Issue 3, 2008

Page: [244 - 249] Pages: 6

DOI: 10.2174/092986608783744289

Price: $65


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.

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

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