4ra6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of linker less Pyrococcus furiosus L-asparaginase== | |
| + | <StructureSection load='4ra6' size='340' side='right'caption='[[4ra6]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ra6]] is a 4 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=4RA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RA6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.503Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4ra6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ra6 OCA], [https://pdbe.org/4ra6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ra6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ra6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ra6 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 == | ||
| + | Covalent linkers bridging the domains of multidomain proteins are considered to be crucial for assembly and function. In this report, an exception in which the linker of a two-domain dimeric L-asparaginase from Pyrococcus furiosus (PfA) was found to be dispensable is presented. Domains of this enzyme assembled without the linker into a conjoined tetrameric form that exhibited higher activity than the parent enzyme. The global shape and quaternary structure of the conjoined PfA were also similar to the wild-type PfA, as observed by their solution scattering profiles and X-ray crystallographic data. Comparison of the crystal structures of substrate-bound and unbound enzymes revealed an altogether new active-site composition and mechanism of action. Thus, conjoined PfA is presented as a unique enzyme obtained through noncovalent, linker-less assembly of constituent domains that is stable enough to function efficiently at elevated temperatures. | ||
| - | + | Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains.,Tomar R, Sharma P, Srivastava A, Bansal S, Kundu B Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3187-97. doi:, 10.1107/S1399004714023414. Epub 2014 Nov 22. PMID:25478837<ref>PMID:25478837</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4ra6" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Asparaginase 3D structures|Asparaginase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus furiosus DSM 3638]] | ||
| + | [[Category: Ashish]] | ||
| + | [[Category: Kundu B]] | ||
| + | [[Category: Sharma P]] | ||
| + | [[Category: Tomar R]] | ||
Current revision
Crystal structure of linker less Pyrococcus furiosus L-asparaginase
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