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| | <StructureSection load='4pga' size='340' side='right'caption='[[4pga]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4pga' size='340' side='right'caption='[[4pga]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pga]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_7a Pseudomonas 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PGA FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pga OCA], [http://pdbe.org/4pga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pga RCSB], [http://www.ebi.ac.uk/pdbsum/4pga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pga 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=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> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ASPQ_PSES7 ASPQ_PSES7] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Glutaminase|Glutaminase]] | + | *[[Glutaminase 3D structures|Glutaminase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas 7a]] | + | [[Category: Pseudomonas sp. 7A]] |
| - | [[Category: Jakob, C G]] | + | [[Category: Jakob CG]] |
| - | [[Category: Lacount, M W]] | + | [[Category: Lacount MW]] |
| - | [[Category: Lebioda, L]] | + | [[Category: Lebioda L]] |
| - | [[Category: Lewinski, K]] | + | [[Category: Lewinski K]] |
| - | [[Category: Roberts, J]] | + | [[Category: Roberts J]] |
| - | [[Category: Bacterial amidohydrolase]]
| + | |
| Structural highlights
Function
ASPQ_PSES7
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jakob CG, Lewinski K, LaCount MW, Roberts J, Lebioda L. 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. Biochemistry. 1997 Jan 28;36(4):923-31. PMID:9020792 doi:10.1021/bi961979x
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