Structural highlights
Publication Abstract from PubMed
Structural comparison indicates the loop region between beta3 and beta4 of SsArd1 was more extended than corresponding region of mesophilic Nats and formed a plastically hydrogen bond network mainly via two Ser residues. Strikingly, two single-point mutants showed ~3 degrees C decrease in melting temperature, while two other variants showed a ~7 degrees C decrease in melting temperature, which correlated to the seriously reducing enzymatic activity. To our knowledge, this is the first discovery of a loop region capable of remarkably improving protein thermostability and to provide a novel possibility to engineer heat-resistant proteins.
Multiple conformations of the loop region confers heat-resistance of SsArd1, a thermophilic NatA.,Chang YY, Hsu CH Chembiochem. 2015 Nov 23. doi: 10.1002/cbic.201500568. PMID:26593285[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chang YY, Hsu CH. Multiple conformations of the loop region confers heat-resistance of SsArd1, a thermophilic NatA. Chembiochem. 2015 Nov 23. doi: 10.1002/cbic.201500568. PMID:26593285 doi:http://dx.doi.org/10.1002/cbic.201500568
