Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story

Life

Alessio Ausili¹  Maria Staiano¹  Jonathan Dattelbaum²  Antonio Varriale¹  Alessandro Capo¹ 

[1] Laboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy; E-Mails:;Department of Chemistry, University of Richmond, Richmond, VA 23173, USA; E-Mail:

关键词: ABC transporters;    periplasmic binding proteins;    arginine;    structural stability;    unfolding;   

DOI  :  10.3390/life3010149

来源: mdpi

【 摘 要 】

Arginine-binding protein from the extremophile Thermotoga maritima is a 27.7 kDa protein possessing the typical two-domain structure of the periplasmic binding proteins family. The protein is characterized by a very high specificity and affinity to bind to arginine, also at high temperatures. Due to its features, this protein could be taken into account as a potential candidate for the design of a biosensor for arginine. It is important to investigate the stability of proteins when they are used for biotechnological applications. In this article, we review the structural and functional features of an arginine-binding protein from the extremophile Thermotoga maritima with a particular eye on its potential biotechnological applications.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.