4pga

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[[Image:4pga.jpg|left|200px]]
 
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{{Structure
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==GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A==
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|PDB= 4pga |SIZE=350|CAPTION= <scene name='initialview01'>4pga</scene>, resolution 1.7&Aring;
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<StructureSection load='4pga' size='340' side='right'caption='[[4pga]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AS1:Description+Not+Provided'>AS1</scene> and <scene name='pdbsite=AS2:Description+Not+Provided'>AS2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NH4:AMMONIUM ION'>NH4</scene>
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<table><tr><td colspan='2'>[[4pga]] 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=4PGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PGA FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamin-(asparagin-)ase Glutamin-(asparagin-)ase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.38 3.5.1.38]
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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]] 1.7&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4pga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pga OCA], [https://pdbe.org/4pga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pga RCSB], [https://www.ebi.ac.uk/pdbsum/4pga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pga ProSAT]</span></td></tr>
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</table>
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'''GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A'''
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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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==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/pg/4pga_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=4pga 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 ==
Pseudomonas 7A glutaminase-asparaginase (PGA) catalyzes the hydrolysis of D- and L-isomers of glutamine and asparagine. X-ray quality type-1 crystals of PGA have been obtained from 2.0 M ammonium sulfate. The space group is C222(1) with unit-cell dimensions a = 78.62, b = 135.80, and c = 137.88 A. The tetrameric molecule is located on a crystallographic 2-fold axis, and two subunits form the asymmetric portion of the unit cell. The structure was solved by the molecular replacement method and refined at 1.7 A resolution to an R = 19.9% with a good geometry of the model, G = 0.05. The resultant electron density maps enabled us to resolve individual constituent atoms of most residues and introduce minor revisions to the amino acid sequence. The catalytic loop, Thr20-Gly40, is in the closed conformation with excellent electron density in both subunits. A sulfate ion and an ammonium ion are bound in the substrate binding site and interect with the loop. This interaction appears to be responsible for the observed closed conformation. New arguments supporting Thr20 as the catalytic nucleophile in the asparaginase activity are proposed.
Pseudomonas 7A glutaminase-asparaginase (PGA) catalyzes the hydrolysis of D- and L-isomers of glutamine and asparagine. X-ray quality type-1 crystals of PGA have been obtained from 2.0 M ammonium sulfate. The space group is C222(1) with unit-cell dimensions a = 78.62, b = 135.80, and c = 137.88 A. The tetrameric molecule is located on a crystallographic 2-fold axis, and two subunits form the asymmetric portion of the unit cell. The structure was solved by the molecular replacement method and refined at 1.7 A resolution to an R = 19.9% with a good geometry of the model, G = 0.05. The resultant electron density maps enabled us to resolve individual constituent atoms of most residues and introduce minor revisions to the amino acid sequence. The catalytic loop, Thr20-Gly40, is in the closed conformation with excellent electron density in both subunits. A sulfate ion and an ammonium ion are bound in the substrate binding site and interect with the loop. This interaction appears to be responsible for the observed closed conformation. New arguments supporting Thr20 as the catalytic nucleophile in the asparaginase activity are proposed.
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==About this Structure==
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Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution.,Jakob CG, Lewinski K, LaCount MW, Roberts J, Lebioda L Biochemistry. 1997 Jan 28;36(4):923-31. PMID:9020792<ref>PMID:9020792</ref>
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4PGA is a [[Single protein]] structure of sequence from [http://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=4PGA 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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Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution., Jakob CG, Lewinski K, LaCount MW, Roberts J, Lebioda L, Biochemistry. 1997 Jan 28;36(4):923-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9020792 9020792]
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</div>
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[[Category: Glutamin-(asparagin-)ase]]
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<div class="pdbe-citations 4pga" style="background-color:#fffaf0;"></div>
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[[Category: Pseudomonas sp. 7a]]
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[[Category: Single protein]]
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[[Category: Jakob, C G.]]
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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: Roberts, J.]]
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[[Category: NH4]]
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[[Category: SO4]]
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[[Category: bacterial amidohydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:36 2008''
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==See Also==
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*[[Glutaminase 3D structures|Glutaminase 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: Large Structures]]
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[[Category: Pseudomonas sp. 7A]]
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[[Category: Jakob CG]]
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[[Category: Lacount MW]]
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[[Category: Lebioda L]]
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[[Category: Lewinski K]]
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[[Category: Roberts J]]

Current revision

GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A

PDB ID 4pga

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