5B5U
Crystal structure of truncated Pyrococcus furiosus L-asparaginase with peptide
Summary for 5B5U
| Entry DOI | 10.2210/pdb5b5u/pdb |
| Descriptor | L-asparaginase, LEU-VAL-VAL-ASN, ASPARTIC ACID, ... (8 entities in total) |
| Functional Keywords | truncated pyrococcus furiosus l-asparaginase, linkerless, hydrolase |
| Biological source | Pyrococcus furiosus DSM 3638 More |
| Total number of polymer chains | 4 |
| Total formula weight | 34858.22 |
| Authors | Sharma, P.,Tomar, R.,Nath, S.K.,Kundu, B.,Ashish, F. (deposition date: 2016-05-23, release date: 2017-05-31, Last modification date: 2024-11-13) |
| Primary citation | Sharma, P.,Tomar, R.,Yadav, S.S.,Badmalia, M.D.,Nath, S.K.,Kundu, B. Heat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property. Sci Rep, 10:21702-21702, 2020 Cited by PubMed 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, Leu-Val-Val-Asn (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. PubMed: 33303914DOI: 10.1038/s41598-020-78877-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.61 Å) |
Structure validation
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