Multiple Conformations of the Loop Region Confers Heat-Resistance on SsArd1, a Thermophilic NatA
Journal
ChemBioChem
Journal Volume
17
Journal Issue
3
Start Page
214
End Page
217
ISSN
14394227
Date Issued
2016-02-02
Author(s)
Chang, Yu-Yung
Abstract
Structural comparison indicates that the loop region between β3 and β4 of SsArd1 is extended relative to the corresponding region in mesophilic Nats, and forms a plastic hydrogen-bond network mainly at two serine residues. Strikingly, two single-point mutants showed ∼3 °C decrease in melting temperature, and two other variants showed ∼7 °C decrease; this correlated with significantly reduced enzymatic activity. To our knowledge, this is the first discovery of a loop region capable of remarkably improving protein thermostability. This provides a novel route to engineer heat-resistant proteins.
Subjects
acetyltransferase
biophysics
crystallization
enzymes
thermostability
Publisher
Wiley-VCH Verlag
Type
journal article