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4nje

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==Crystal structure of Pyrococcus furiosus L-asparaginase with ligand==
==Crystal structure of Pyrococcus furiosus L-asparaginase with ligand==
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<StructureSection load='4nje' size='340' side='right' caption='[[4nje]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4nje' size='340' side='right'caption='[[4nje]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nje]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NJE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nje]] 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=4NJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NJE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
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<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=4nje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nje OCA], [http://pdbe.org/4nje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nje RCSB], [http://www.ebi.ac.uk/pdbsum/4nje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nje ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nje OCA], [https://pdbe.org/4nje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nje RCSB], [https://www.ebi.ac.uk/pdbsum/4nje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nje ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4nje" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Asparaginase|Asparaginase]]
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*[[Asparaginase 3D structures|Asparaginase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Asparaginase]]
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[[Category: Large Structures]]
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[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Ashish]]
[[Category: Ashish]]
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[[Category: Kundu, B]]
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[[Category: Kundu B]]
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[[Category: Sharma, P]]
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[[Category: Sharma P]]
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[[Category: Singh, S]]
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[[Category: Singh S]]
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[[Category: Tomar, R]]
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[[Category: Tomar R]]
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[[Category: Yadav, S P.S]]
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[[Category: Yadav SPS]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of Pyrococcus furiosus L-asparaginase with ligand

PDB ID 4nje

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