Sharma, Pankaj and Tomar, Rachana and Yadav, Shiv Pratap Singh and Badmalia, Maulik D and Nath, Samir K and Ashish, . and Kundu, Bishwajit (2020) Heat induces end to end repetitive association in P. furiosusl-asparaginase which enables its thermophilic property. Scientific reports, 10. ISSN 2045-2322
Full text not available from this repository. (Request a copy)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 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.
| Item Type: | Article |
|---|---|
| Additional Information: | Open Access |
| Uncontrolled Keywords: | Biophysics, Structural biology |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 31 Dec 2020 11:17 |
| Last Modified: | 31 Dec 2020 11:17 |
| URI: | http://crdd.osdd.net/open/id/eprint/2634 |
Actions (login required)
 |
View Item |
