5cbp: Difference between revisions

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 <StructureSection load='5cbp' size='340' side='right'caption='[[5cbp]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5cbp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CBP FirstGlance]. <br>
+<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]] 2.358&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF2047, ph0066 ([http://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=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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbp OCA], [http://pdbe.org/5cbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cbp RCSB], [http://www.ebi.ac.uk/pdbsum/5cbp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbp 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=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>
+== 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&reg;/PubMed&reg;, 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__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Pyrfu]]
+[[Category: Pyrococcus furiosus DSM 3638]]
-[[Category: Ashish, F]]
+[[Category: Ashish F]]
-[[Category: Kundu, B]]
+[[Category: Kundu B]]
-[[Category: Sharma, P]]
+[[Category: Sharma P]]
-[[Category: Tomar, R]]
+[[Category: Tomar R]]
-[[Category: Yadav, S P]]
+[[Category: Yadav SP]]
-[[Category: Hydrolase]]