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==Asparaginase II from Escherichia coli==
==Asparaginase II from Escherichia coli==
<StructureSection load='6uoh' size='340' side='right'caption='[[6uoh]]' scene=''>
<StructureSection load='6uoh' size='340' side='right'caption='[[6uoh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UOH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UOH FirstGlance]. <br>
<table><tr><td colspan='2'>[[6uoh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UOH FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6uoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uoh OCA], [http://pdbe.org/6uoh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uoh RCSB], [http://www.ebi.ac.uk/pdbsum/6uoh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uoh ProSAT]</span></td></tr>
</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></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ansB, b2957, JW2924 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [https://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=6uoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uoh OCA], [https://pdbe.org/6uoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uoh RCSB], [https://www.ebi.ac.uk/pdbsum/6uoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uoh ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hydrolysis of asparagine and glutamine by L-asparaginase has been used to treat acute lymphoblastic leukemia for over four decades. Each L-asparaginase monomer has a long loop that closes over the active site upon substrate binding, acting as a lid. Here we present a comparative study of two commercially available preparations of the drug containing Escherichia coli L-Asparaginase 2 (EcA2), performed by a comprehensive array of biophysical and biochemical approaches. We report the oligomeric landscape and conformational and dynamic plasticity of E. coli type 2 L-asparaginase present in two different formulations, and its relationship with L-aspartic acid, which is present in Aginasa, but not in Leuginase. The L-Asp present in Aginasa formulation was found to provide to EcA2 a resistance to in vitro proteolysis. EcA2 shows a composition of monomers and oligomers up to tetramers, which is mostly not altered in the presence of L-Asp. Ion-mobility spectrometry-mass spectrometry reveals two conformers for the monomeric EcA2, and that monomeric species has sufficient capacity for selective binding to L-Asp and L-Glu. The N-terminal loop of the EcA2 present in Leuginase, which is part of the active site is disordered, but it gets ordered in the presence of L-Asp, while L-Glu only does so to a limited extent. These data provide new insights on the mechanistic of ligand recognition by EcA2, and the impact of formulation in its conformational diversity landscape.
Biophysical characterization of two commercially available preparations of the drug containing Escherichia coli L-Asparaginase 2.,de Araujo TS, Scapin SMN, de Andrade W, Fasciotti M, de Magalhaes MTQ, Almeida MS, Lima LMTR Biophys Chem. 2021 Feb 5;271:106554. doi: 10.1016/j.bpc.2021.106554. PMID:33607531<ref>PMID:33607531</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6uoh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Asparaginase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Almeida MS]]
[[Category: Almeida, M S]]
[[Category: Araujo TS]]
[[Category: Araujo, T S]]
[[Category: Lima LMTR]]
[[Category: Lima, L M.T R]]
[[Category: Acute lymphoblastic leukemia]]
[[Category: Cancer]]
[[Category: Hydrolase]]
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