Heat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property.

ABSTRACT: It remains undeciphered how thermophilic enzymes display enhanced stability at elevated temperatures. Taking L-asparaginase from P. furiosus (PfA) as an example, we combined scattering shapes deduced from small-angle X-ray scattering (SAXS) data at increased temperatures with symmetry mates from crystallographic structures to find that heating caused end-to-end association. The small contact point of self-binding appeared to be enabled by a terminal short β-strand in N-terminal domain, Leu¹⁷⁹-Val-Val-Asn¹⁸² (LVVN). Interestingly, deletion of this strand led to a defunct enzyme, whereas suplementation of the peptide LVVN to the defunct enzyme restored structural frameworkwith mesophile-type functionality. Crystal structure of the peptide-bound defunct enzyme showed tha

SUBMITTER: Sharma P 

PROVIDER: S-EPMC7728782 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature