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| | <StructureSection load='2vur' size='340' side='right'caption='[[2vur]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2vur' size='340' side='right'caption='[[2vur]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vur]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VUR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vur]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VUR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YX1:2-DEOXY-2-{[(2-HYDROXY-1-METHYLHYDRAZINO)CARBONYL]AMINO}-BETA-D-GLUCOPYRANOSE'>YX1</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j62|2j62]], [[2jh2|2jh2]], [[2v5c|2v5c]], [[2v5d|2v5d]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YX1:2-DEOXY-2-{[(2-HYDROXY-1-METHYLHYDRAZINO)CARBONYL]AMINO}-BETA-D-GLUCOPYRANOSE'>YX1</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </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=2vur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vur OCA], [https://pdbe.org/2vur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vur RCSB], [https://www.ebi.ac.uk/pdbsum/2vur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vur ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vur OCA], [http://pdbe.org/2vur PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vur RCSB], [http://www.ebi.ac.uk/pdbsum/2vur PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vur ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. | + | [https://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] |
| | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] |
| | + | *[[O-GlcNAcase|O-GlcNAcase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus perfringens veillon and zuber 1898]] | + | [[Category: Clostridium perfringens]] |
| - | [[Category: Hydrolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aalten, D M.F van]]
| + | [[Category: Borodkin VS]] |
| - | [[Category: Borodkin, V S]] | + | [[Category: Dorfmueller HC]] |
| - | [[Category: Dorfmueller, H C]] | + | [[Category: Pathak S]] |
| - | [[Category: Pathak, S]] | + | [[Category: Van Aalten DMF]] |
| - | [[Category: Glycosidase]] | + | |
| Structural highlights
Function
OGA_CLOP1 Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
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
Streptozotocin is a natural product that selectively kills insulin-secreting beta cells, and is widely used to generate mouse models of diabetes or treat pancreatic tumors. Several studies suggest that streptozotocin toxicity stems from its N-nitrosourea moiety releasing nitric oxide and possessing DNA alkylating activity. However, it has also been proposed that streptozotocin induces apoptosis by inhibiting O-GlcNAcase, an enzyme that, together with O-GlcNAc transferase, is important for dynamic intracellular protein O-glycosylation. We have used galacto-streptozotocin to chemically dissect the link between O-GlcNAcase inhibition and apoptosis. Using X-ray crystallography, enzymology, and cell biological studies on an insulinoma cell line, we show that, whereas streptozotocin competitively inhibits O-GlcNAcase and induces apoptosis, its galacto-configured derivative no longer inhibits O-GlcNAcase, yet still induces apoptosis. This supports a general chemical poison mode of action for streptozotocin, suggesting the need for using more specific inhibitors to study protein O-GlcNAcylation.
Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death.,Pathak S, Dorfmueller HC, Borodkin VS, van Aalten DM Chem Biol. 2008 Aug 25;15(8):799-807. PMID:18721751[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pathak S, Dorfmueller HC, Borodkin VS, van Aalten DM. Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death. Chem Biol. 2008 Aug 25;15(8):799-807. PMID:18721751 doi:10.1016/j.chembiol.2008.06.010
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