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Multiple Conformations of the Loop Region Confers Heat‐Resistance on SsArd1, a Thermophilic NatA
Author(s) -
Chang YuYung,
Hsu ChunHua
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500568
Subject(s) - thermostability , thermophile , mesophile , loop (graph theory) , hydrogen bond , mutant , chemistry , serine , heat resistance , enzyme , biochemistry , crystallography , materials science , biology , molecule , genetics , organic chemistry , gene , mathematics , combinatorics , bacteria , composite material
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.