2jk0: Difference between revisions
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<StructureSection load='2jk0' size='340' side='right'caption='[[2jk0]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2jk0' size='340' side='right'caption='[[2jk0]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jk0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2jk0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JK0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jk0 OCA], [https://pdbe.org/2jk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jk0 RCSB], [https://www.ebi.ac.uk/pdbsum/2jk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jk0 ProSAT]</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=2jk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jk0 OCA], [https://pdbe.org/2jk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jk0 RCSB], [https://www.ebi.ac.uk/pdbsum/2jk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jk0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6Q4F4_PECAT Q6Q4F4_PECAT] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pectobacterium carotovorum]] | ||
[[Category: | [[Category: Andersson CS]] | ||
[[Category: | [[Category: Krasotkina J]] | ||
[[Category: | [[Category: Papageorgiou AC]] | ||
[[Category: | [[Category: Posypanova GA]] | ||
[[Category: | [[Category: Sokolov NN]] | ||
Latest revision as of 17:52, 13 December 2023
Structural and functional insights into Erwinia carotovora L- asparaginaseStructural and functional insights into Erwinia carotovora L- asparaginase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacterial L-asparaginases are enzymes that catalyze the hydrolysis of l-asparagine to aspartic acid. For the past 30 years, these enzymes have been used as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia. Their intrinsic low-rate glutaminase activity, however, causes serious side-effects, including neurotoxicity, hepatitis, coagulopathy, and other dysfunctions. Erwinia carotovora asparaginase shows decreased glutaminase activity, so it is believed to have fewer side-effects in leukemia therapy. To gain detailed insights into the properties of E. carotovora asparaginase, combined crystallographic, thermal stability and cytotoxic experiments were performed. The crystal structure of E. carotovoral-asparaginase in the presence of L-Asp was determined at 2.5 A resolution and refined to an R cryst of 19.2 (R free = 26.6%) with good stereochemistry. Cytotoxicity measurements revealed that E. carotovora asparaginase is 30 times less toxic than the Escherichia coli enzyme against human leukemia cell lines. Moreover, denaturing experiments showed that E. carotovora asparaginase has decreased thermodynamic stability as compared to the E. coli enzyme and is rapidly inactivated in the presence of urea. On the basis of these results, we propose that E. carotovora asparaginase has limited potential as an antileukemic drug, despite its promising low glutaminase activity. Our analysis may be applicable to the therapeutic evaluation of other asparaginases as well. Structural and functional insights into Erwinia carotovora L-asparaginase.,Papageorgiou AC, Posypanova GA, Andersson CS, Sokolov NN, Krasotkina J FEBS J. 2008 Sep;275(17):4306-16. Epub 2008 Jul 21. PMID:18647344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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