TY  - JOUR
N1  - Open Access
ID  - open2634
UR  - https://www.nature.com/articles/s41598-020-78877-z
A1  - Sharma, Pankaj
A1  - Tomar, Rachana
A1  - Yadav, Shiv Pratap Singh
A1  - Badmalia, Maulik D
A1  - Nath, Samir K
A1  - Ashish, .
A1  - Kundu, Bishwajit
Y1  - 2020/12/10/
N2  - 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 ?-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 that one peptide ispresent in the same coordinates as in original enzyme, explaining gain-of lost function. A second peptide was seen bound to the protein at a different location suggesting its possible role in substrate-free molecular-association. Overall, we show that the heating induced self-assembly of native shapes of PfA led to an apparent super-stable assembly.
PB  - Nature publishing group
JF  - Scientific reports
VL  - 10
KW  - Biophysics
KW  -  Structural biology
SN  - 2045-2322
TI  - Heat induces end to end repetitive association in P. furiosusl-asparaginase which enables its thermophilic property
ER  -