Heat induces end to end repetitive association in P. furiosusl-asparaginase which enables its thermophilic property
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
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| Title |
Heat induces end to end repetitive association in P. furiosusl-asparaginase which enables its thermophilic property
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| Creator |
Sharma, Pankaj
Tomar, Rachana Yadav, Shiv Pratap Singh Badmalia, Maulik D Nath, Samir K Ashish, . Kundu, Bishwajit |
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| Subject |
QR Microbiology
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| Description |
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.
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| Publisher |
Nature publishing group
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| Date |
2020-12-10
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| Type |
Article
PeerReviewed |
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| Relation |
https://www.nature.com/articles/s41598-020-78877-z
http://crdd.osdd.net/open/2634/ |
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| Identifier |
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
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