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| | <StructureSection load='5b74' size='340' side='right'caption='[[5b74]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='5b74' size='340' side='right'caption='[[5b74]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b74]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B74 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b74]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] and [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B74 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.039Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF2047 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b74 OCA], [https://pdbe.org/5b74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b74 RCSB], [https://www.ebi.ac.uk/pdbsum/5b74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b74 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b74 OCA], [https://pdbe.org/5b74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b74 RCSB], [https://www.ebi.ac.uk/pdbsum/5b74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b74 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ASPG_PYRFU ASPG_PYRFU] Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Displays no glutaminase activity, a highly desirable therapeutic property.<ref>PMID:20370616</ref> <ref>PMID:22166247</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Asparaginase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyrfu]] | + | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Ashish, F]] | + | [[Category: Pyrococcus furiosus DSM 3638]] |
| - | [[Category: Kundu, B]] | + | [[Category: Ashish F]] |
| - | [[Category: Nath, S K]] | + | [[Category: Kundu B]] |
| - | [[Category: Sharma, P]] | + | [[Category: Nath SK]] |
| - | [[Category: Tomar, R]] | + | [[Category: Sharma P]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Tomar R]] |
| - | [[Category: Linkerless]]
| + | |
| - | [[Category: Truncated pyrococcus furiosus l-asparaginase]]
| + | |
| Structural highlights
Function
ASPG_PYRFU Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Displays no glutaminase activity, a highly desirable therapeutic property.[1] [2]
Publication Abstract from PubMed
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 beta-strand in N-terminal domain, Leu(179)-Val-Val-Asn(182) (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.
Heat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property.,Sharma P, Tomar R, Yadav SS, Badmalia MD, Nath SK, Ashish, Kundu B Sci Rep. 2020 Dec 10;10(1):21702. doi: 10.1038/s41598-020-78877-z. PMID:33303914[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bansal S, Gnaneswari D, Mishra P, Kundu B. Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochemistry (Mosc). 2010 Mar;75(3):375-81. doi: 10.1134/s0006297910030144. PMID:20370616 doi:http://dx.doi.org/10.1134/s0006297910030144
- ↑ Bansal S, Srivastava A, Mukherjee G, Pandey R, Verma AK, Mishra P, Kundu B. Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action. FASEB J. 2012 Mar;26(3):1161-71. doi: 10.1096/fj.11-191254. Epub 2011 Dec 13. PMID:22166247 doi:http://dx.doi.org/10.1096/fj.11-191254
- ↑ Sharma P, Tomar R, Yadav SS, Badmalia MD, Nath SK, Ashish, Kundu B. Heat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property. Sci Rep. 2020 Dec 10;10(1):21702. doi: 10.1038/s41598-020-78877-z. PMID:33303914 doi:http://dx.doi.org/10.1038/s41598-020-78877-z
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