3uo9

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Crystal Structure of Human GAC in Complex with Glutamate and BPTES

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 <StructureSection load='3uo9' size='340' side='right'caption='[[3uo9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uo9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UO9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uo9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UO9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04A:N,N-[SULFANEDIYLBIS(ETHANE-2,1-DIYL-1,3,4-THIADIAZOLE-5,2-DIYL)]BIS(2-PHENYLACETAMIDE)'>04A</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3unw|3unw]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04A:N,N-[SULFANEDIYLBIS(ETHANE-2,1-DIYL-1,3,4-THIADIAZOLE-5,2-DIYL)]BIS(2-PHENYLACETAMIDE)'>04A</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLS, GLS1, KIAA0838 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutaminase Glutaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.2 3.5.1.2] </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=3uo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uo9 OCA], [https://pdbe.org/3uo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uo9 RCSB], [https://www.ebi.ac.uk/pdbsum/3uo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uo9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GLSK_HUMAN GLSK_HUMAN]] Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.
+[https://www.uniprot.org/uniprot/GLSK_HUMAN GLSK_HUMAN] Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Glutaminase (GLS1/2) catalyzes the conversion of l-glutamine to l-glutamate and ammonia. The level of a splice variant of GLS1 (GAC) is elevated in certain cancers, and GAC is specifically inhibited by bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide (BPTES). We report here the first full-length crystal structure of GAC in the presence and absence of BPTES molecules. Two BPTES molecules bind at an interface region of the GAC tetramer in a manner that appears to lock the GAC tetramer into a nonproductive conformation. The importance of these loops with regard to overall enzymatic activity of the tetramer was revealed by a series of GAC point mutants designed to create a BPTES resistant GAC.
-Full-Length Human Glutaminase in Complex with an Allosteric Inhibitor.,Delabarre B, Gross S, Fang C, Gao Y, Jha A, Jiang F, Song J J, Wei W, Hurov JB Biochemistry. 2011 Nov 18. PMID:22049910<ref>PMID:22049910</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3uo9" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Glutaminase 3D structures|Glutaminase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Glutaminase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Cheng, F]]
+[[Category: Cheng F]]
-[[Category: DeLaBarre, B]]
+[[Category: DeLaBarre B]]
-[[Category: Gao, Y]]
+[[Category: Gao Y]]
-[[Category: Gross, S]]
+[[Category: Gross S]]
-[[Category: Hurov, J B]]
+[[Category: Hurov JB]]
-[[Category: Jha, A]]
+[[Category: Jha A]]
-[[Category: Jiang, F]]
+[[Category: Jiang F]]
-[[Category: Song, J J]]
+[[Category: Song JJ]]
-[[Category: Wei, W]]
+[[Category: Wei W]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]

3uo9

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Current revision

Crystal Structure of Human GAC in Complex with Glutamate and BPTES

Structural highlights

Function

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