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Biological function in a non‐native partially folded state of a protein
Author(s) -
Bemporad Francesco,
Gsponer Joerg,
Hopearuoho Harri I,
Plakoutsi Georgia,
Stati Gianmarco,
Stefani Massimo,
Taddei Niccolò,
Vendruscolo Michele,
Chiti Fabrizio
Publication year - 2008
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2008.82
Subject(s) - function (biology) , native state , state (computer science) , computational biology , chemistry , biophysics , biology , computer science , evolutionary biology , biochemistry , algorithm
As structural flexibility is known to be required for enzyme catalysis and pattern recognition and a significant fraction of eukaryotic proteins appear to be unfolded or contain unstructured regions, biological activity of conformational states distinct from fully folded structures could be more common than previously thought. By applying a procedure that allows the recovery of enzymatic activity to be monitored in real time, we show that a non‐native state populated transiently during folding of the acylphosphatase from Sulfolobus solfataricus is enzymatically active. The structural characterization of this partially folded state reveals that enzymatic activity is possible even if the catalytic site is structurally heterogeneous, whereas the remainder of the structure acts as a scaffold. These results extend the spectrum of biological functions carried out in the absence of a folded state to include enzyme catalysis.