8ecd: Difference between revisions
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==E. coli L-asparaginase II mutant (V27T) in complex with L-Asp== | |||
<StructureSection load='8ecd' size='340' side='right'caption='[[8ecd]], [[Resolution|resolution]] 1.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ecd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ECD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ECD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=8ecd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ecd OCA], [https://pdbe.org/8ecd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ecd RCSB], [https://www.ebi.ac.uk/pdbsum/8ecd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ecd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ASPG2_ECOLI ASPG2_ECOLI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial L-asparaginases have been used for over 40 years as anticancer drugs. Ardalan et al. (Medical Hypotheses 112, 7-17, 2018) proposed that the V27T mutant of Escherichia coli type II L-asparaginase, EcAII(V27T), should display altered biophysical and catalytic properties compared to the wild-type enzyme, EcAII(wt), rendering it more favourable as a pharmaceutical. They postulated that EcAII(V27T) would exhibit reduced glutaminolytic activity and be more stable compared to EcAII(wt). Their postulates, however, were purely theoretical. Here, we characterized experimentally selected properties of EcAII(V27T). We found asparaginolytic activity of this mutant unchanged, whereas its glutaminolytic activity was fourfold lower compared with EcAII(wt). We did not observe significant differences in stabilities of EcAII(wt) and EcAII(V27T). Crystal structures of the complexes with L-Asp and L-Glu showed considerable differences in binding modes of both substrates. | |||
The E. coli L-asparaginase V27T mutant: structural and functional characterization and comparison with theoretical predictions.,Strzelczyk P, Zhang D, Wlodawer A, Lubkowski J FEBS Lett. 2022 Oct 30. doi: 10.1002/1873-3468.14526. PMID:36310372<ref>PMID:36310372</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ecd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Lubkowski J]] | |||
[[Category: Strzelczyk P]] | |||
[[Category: Wlodawer A]] | |||
Revision as of 23:16, 16 November 2022
E. coli L-asparaginase II mutant (V27T) in complex with L-AspE. coli L-asparaginase II mutant (V27T) in complex with L-Asp
Structural highlights
FunctionPublication Abstract from PubMedBacterial L-asparaginases have been used for over 40 years as anticancer drugs. Ardalan et al. (Medical Hypotheses 112, 7-17, 2018) proposed that the V27T mutant of Escherichia coli type II L-asparaginase, EcAII(V27T), should display altered biophysical and catalytic properties compared to the wild-type enzyme, EcAII(wt), rendering it more favourable as a pharmaceutical. They postulated that EcAII(V27T) would exhibit reduced glutaminolytic activity and be more stable compared to EcAII(wt). Their postulates, however, were purely theoretical. Here, we characterized experimentally selected properties of EcAII(V27T). We found asparaginolytic activity of this mutant unchanged, whereas its glutaminolytic activity was fourfold lower compared with EcAII(wt). We did not observe significant differences in stabilities of EcAII(wt) and EcAII(V27T). Crystal structures of the complexes with L-Asp and L-Glu showed considerable differences in binding modes of both substrates. The E. coli L-asparaginase V27T mutant: structural and functional characterization and comparison with theoretical predictions.,Strzelczyk P, Zhang D, Wlodawer A, Lubkowski J FEBS Lett. 2022 Oct 30. doi: 10.1002/1873-3468.14526. PMID:36310372[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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