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1djo

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[[Image:1djo.gif|left|200px]]
 
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==Crystal structure of Pseudomonas 7A Glutaminase-asparaginase with the inhibitor donv covalently bound in the active site==
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The line below this paragraph, containing "STRUCTURE_1djo", creates the "Structure Box" on the page.
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<StructureSection load='1djo' size='340' side='right'caption='[[1djo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1djo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._7A Pseudomonas sp. 7A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAB:4,4-DIHYDROXY-5-OXO-L-NORVALINE'>CAB</scene></td></tr>
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{{STRUCTURE_1djo| PDB=1djo | SCENE= }}
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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=1djo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1djo OCA], [https://pdbe.org/1djo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1djo RCSB], [https://www.ebi.ac.uk/pdbsum/1djo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1djo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASPQ_PSES7 ASPQ_PSES7]
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== Evolutionary Conservation ==
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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/dj/1djo_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=1djo ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE WITH THE INHIBITOR DONV COVALENTLY BOUND IN THE ACTIVE SITE'''
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==See Also==
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*[[Glutaminase 3D structures|Glutaminase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Pseudomonas 7A glutaminase-asparaginase (PGA) catalyzes the hydrolysis of D and L isomers of glutamine and asparagine. Crystals of PGA were reacted with diazo analogues of glutamine (6-diazo-5-oxo-L-norleucine, DON) and asparagine (5-diazo-4-oxo-L-norvaline, DONV), which are known inhibitors of the enzyme. The derivatized crystals remained isomorphous to native PGA crystals. Their structures were refined to crystallographic R = 0.20 and R(free) = 0.24 for PGA-DON and R = 0.19 and R = 0.23 for PGA-DONV. Difference Fourier electron density maps clearly showed that both DON and DONV inactivate PGA through covalent inhibition. Continuous electron density connecting the inhibitor to both Thr20 and Tyr34 of the flexible loop was observed providing strong evidence that Thr20 is the primary catalytic nucleophile and that Tyr34 plays an important role in catalysis as well. The unexpected covalent binding observed in the PGA-DON and PGA-DONV complexes shows that a secondary reaction involving the formation of a Tyr34-inhibitor bond takes place with concomitant inactivation of PGA. The predicted covalent linkage is not seen, however, suggesting an alternative method of inhibition not yet seen for these diazo analogues. These surprising results give insight as to the role of the flexible loop Thr and Tyr in the catalytic mechanism.
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp. 7A]]
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==About this Structure==
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[[Category: Lacount MW]]
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1DJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJO OCA].
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[[Category: Lebioda L]]
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[[Category: Lewinski K]]
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==Reference==
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[[Category: Ortlund E]]
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Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu., Ortlund E, Lacount MW, Lewinski K, Lebioda L, Biochemistry. 2000 Feb 15;39(6):1199-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10684596 10684596]
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[[Category: Pseudomonas sp.]]
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[[Category: Single protein]]
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[[Category: Lacount, M W.]]
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[[Category: Lebioda, L.]]
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[[Category: Lewinski, K.]]
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[[Category: Ortlund, E.]]
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[[Category: 5-diazo-4-oxo-l-norvaline]]
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[[Category: Asparaginase]]
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[[Category: Covalently bound inhibitor]]
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[[Category: Donv]]
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[[Category: Glutaminase]]
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[[Category: Glutaminase-asparaginase]]
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[[Category: Pga]]
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[[Category: Suicide inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:55:27 2008''
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Current revision

Crystal structure of Pseudomonas 7A Glutaminase-asparaginase with the inhibitor donv covalently bound in the active site

PDB ID 1djo

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