Structural and Functional Characteristics of TIM-Barrel as a Novel Scaffold for protein Design and Engineering

摘要

During the last 25 years, many investigations have been carried out to understand the principles responsible for thefolding and stability of the TIM-barrel fold. Recently the characteristics of TIM-barrel proteins have been reviewed in detail interms of their structure, folding, function, and evolution. The TIM-barrel or (β/α)8-barrel fold is the most common enzyme fold inthe protein data bank (PDB) database of known protein structures. It is seen in many different enzyme families catalysingcompletely unrelated reactions. Some of the most effective enzymes are TIM-barrel enzymes, for example TIM (triose phosphateisomerase) which catalyses an interconversion reaction in the glycosidic pathway. The (β/α)8-barrel fold is of particularinterests for designing novel catalysts because it is the most common topology for enzymes and one of the most diversesuperfolds. Recent efforts have been devoted to de novo-design symmetric and functional TIM-barrels which is ideal for enzymedesign and protein engineering. In this study, we determined the structural and functional characteristics of a de novo-designedTIM-barrel for protein design and engineering purposes.