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==Crystal Structure of Conjoint Pyrococcus Furiosus L-asparaginase with Citrate==
==Crystal Structure of Conjoint Pyrococcus Furiosus L-asparaginase with Citrate==
<StructureSection load='4ra9' size='340' side='right' caption='[[4ra9]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='4ra9' size='340' side='right'caption='[[4ra9]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ra9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RA9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ra9]] 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=4RA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RA9 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]] 2.049&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ra6|4ra6]]</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='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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ra9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ra9 OCA], [https://pdbe.org/4ra9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ra9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ra9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ra9 ProSAT]</span></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=4ra9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ra9 OCA], [http://pdbe.org/4ra9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ra9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ra9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ra9 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 ==
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ra9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Asparaginase|Asparaginase]]
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Asparaginase]]
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Ashish]]
[[Category: Ashish]]
[[Category: Kundu, B]]
[[Category: Kundu B]]
[[Category: Sharma, P]]
[[Category: Sharma P]]
[[Category: Singh, S]]
[[Category: Singh S]]
[[Category: Tomar, R]]
[[Category: Tomar R]]
[[Category: Yadav, S P.S]]
[[Category: Yadav SPS]]
[[Category: Hydrolase]]

Latest revision as of 15:13, 8 November 2023

Crystal Structure of Conjoint Pyrococcus Furiosus L-asparaginase with Citrate

4ra9, resolution 2.05Å

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