@article{open2634,
          volume = {10},
           month = {December},
          author = {Pankaj Sharma and Rachana Tomar and Shiv Pratap Singh Yadav and Maulik D Badmalia and Samir K Nath and . Ashish and Bishwajit Kundu},
            note = {Open Access},
           title = {Heat induces end to end repetitive association in P. furiosusl-asparaginase which enables its thermophilic property},
       publisher = {Nature publishing group},
         journal = {Scientific reports},
            year = {2020},
        keywords = {Biophysics, Structural biology},
             url = {http://crdd.osdd.net/open/2634/},
        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 {\ensuremath{\beta}}-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.}
}