2jk0: Difference between revisions

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-{{Seed}}
-[[Image:2jk0.png|left|200px]]
-<!--
+==Structural and functional insights into Erwinia carotovora L- asparaginase==
-The line below this paragraph, containing "STRUCTURE_2jk0", creates the "Structure Box" on the page.
+<StructureSection load='2jk0' size='340' side='right'caption='[[2jk0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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>
-{{STRUCTURE_2jk0|  PDB=2jk0  |  SCENE=  }}
+<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>
+== Function ==
+[https://www.uniprot.org/uniprot/Q6Q4F4_PECAT Q6Q4F4_PECAT]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jk/2jk0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jk0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacterial 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===
+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<ref>PMID:18647344</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2jk0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18647344}}, adds the Publication Abstract to the page
+*[[Asparaginase 3D structures|Asparaginase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18647344 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18647344}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-JK0 is a 8 chains structure of sequences from [http://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].
-==Reference==
-<ref group="xtra">PMID:18647344</ref><references group="xtra"/>
-[[Category: Asparaginase]]
 [[Category: Pectobacterium carotovorum]]
-[[Category: Andersson, C S.]]
+[[Category: Andersson CS]]
-[[Category: Krasotkina, J.]]
+[[Category: Krasotkina J]]
-[[Category: Papageorgiou, A C.]]
+[[Category: Papageorgiou AC]]
-[[Category: Posypanova, G A.]]
+[[Category: Posypanova GA]]
-[[Category: Sokolov, N N.]]
+[[Category: Sokolov NN]]
-[[Category: Enzyme therapy]]
-[[Category: Erwinia]]
-[[Category: Hydrolase]]
-[[Category: Leukemia treatment]]
-[[Category: Protein stability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:00:07 2009''