In this paper Barbara Zambelli and colleagues discuss the first known intrinsically disordered enzyme which exhibits activity in its disordered state. This protein, BpUreG, from Bacillus pasteurii exists in three different forms depending on the temperature and concentration of denaturant used.
Intrinsic disorder is well known to play a role in some key regulative functions in proteins, while enzymatic activity is generally associated with overall protein rigidity, and only few cases of artificial intrinsically disordered enzymes have been reported so far. The present study provides insights into the folding landscape sampled by BpUreG, the first discovered native intrinsically disordered enzyme, known to be active in its unstructured state. A combination of spectroscopic and calorimetric techniques revealed that this enzyme exists as an ensemble of uncooperatively interconverting conformational states, whose degree of structure depends on temperature and denaturant concentration.
- Barbara Zambelli
Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme
Barbara Zambelli, Nunilo Cremades, Paolo Neyroz, Paola Turano, Vladimir N. Uversky and Stefano Ciurli
Mol. BioSyst., 2012, Advance Article
DOI: 10.1039/C1MB05227F, Paper
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