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==Crystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree C== | ==Crystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree C== | ||
<StructureSection load='5cbp' size='340' side='right' caption='[[5cbp]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='5cbp' size='340' side='right'caption='[[5cbp]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cbp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CBP OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5cbp]] is a 2 chain structure with sequence from [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=5CBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CBP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 2.358Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></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=5cbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbp OCA], [https://pdbe.org/5cbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cbp RCSB], [https://www.ebi.ac.uk/pdbsum/5cbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbp 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;"> | |||
== 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<ref>PMID:33303914</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5cbp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Asparaginase 3D structures|Asparaginase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ashish | [[Category: Large Structures]] | ||
[[Category: Kundu | [[Category: Pyrococcus furiosus DSM 3638]] | ||
[[Category: Sharma | [[Category: Ashish F]] | ||
[[Category: Tomar | [[Category: Kundu B]] | ||
[[Category: Yadav | [[Category: Sharma P]] | ||
[[Category: Tomar R]] | |||
[[Category: Yadav SP]] | |||
Latest revision as of 19:08, 8 November 2023
Crystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree CCrystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree C
Structural highlights
FunctionASPG_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 PubMedIt 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 AlsoReferences
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