8ece

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'''Unreleased structure'''
 
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The entry 8ece is ON HOLD
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==E. coli L-asparaginase II mutant (V27T) in complex with L-Glu==
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<StructureSection load='8ece' size='340' side='right'caption='[[8ece]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ece]] 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=8ECE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ECE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></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=8ece FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ece OCA], [https://pdbe.org/8ece PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ece RCSB], [https://www.ebi.ac.uk/pdbsum/8ece PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ece ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASPG2_ECOLI ASPG2_ECOLI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8ece" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Lubkowski J]]
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[[Category: Strzelczyk P]]
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[[Category: Wlodawer A]]

Revision as of 20:17, 16 November 2022

E. coli L-asparaginase II mutant (V27T) in complex with L-Glu

PDB ID 8ece

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