4eca

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[[Image:4eca.jpg|left|200px]]
 
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{{Structure
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==ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE==
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|PDB= 4eca |SIZE=350|CAPTION= <scene name='initialview01'>4eca</scene>, resolution 2.2&Aring;
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<StructureSection load='4eca' size='340' side='right'caption='[[4eca]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AS:Active+Site+In+Monomer+A'>AS</scene>, <scene name='pdbsite=BS:Active+Site+In+Monomer+B'>BS</scene>, <scene name='pdbsite=CS:Active+Site+In+Monomer+C'>CS</scene> and <scene name='pdbsite=DS:Active+Site+In+Monomer+D'>DS</scene>
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[4eca]] 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=4ECA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ECA FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE= ANSB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AEI:THREONINE-ASPARTIC+ESTER'>AEI</scene></td></tr>
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}}
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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=4eca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eca OCA], [https://pdbe.org/4eca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eca RCSB], [https://www.ebi.ac.uk/pdbsum/4eca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eca ProSAT]</span></td></tr>
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</table>
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'''ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE'''
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== Function ==
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[https://www.uniprot.org/uniprot/ASPG2_ECOLI ASPG2_ECOLI]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ec/4eca_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=4eca ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly inactive mutant in which one of the active site threonines, Thr-89, was replaced by valine was constructed, expressed, and crystallized. Its structure, solved at 2.2 A resolution, shows high overall similarity to the wild-type enzyme, but an aspartyl moiety is covalently bound to Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail.
Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly inactive mutant in which one of the active site threonines, Thr-89, was replaced by valine was constructed, expressed, and crystallized. Its structure, solved at 2.2 A resolution, shows high overall similarity to the wild-type enzyme, but an aspartyl moiety is covalently bound to Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail.
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==About this Structure==
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A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant.,Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:8706862<ref>PMID:8706862</ref>
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4ECA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ECA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant., Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A, FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8706862 8706862]
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</div>
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[[Category: Asparaginase]]
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<div class="pdbe-citations 4eca" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Lubkowski, J.]]
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[[Category: Palm, G J.]]
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[[Category: Wlodawer, A.]]
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[[Category: acyl-enzyme intermediate]]
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[[Category: hydrolase]]
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[[Category: threonine amidohydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:09:31 2008''
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==See Also==
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*[[Asparaginase 3D structures|Asparaginase 3D structures]]
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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: Palm GJ]]
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[[Category: Wlodawer A]]

Current revision

ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE

PDB ID 4eca

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