2x0h: Difference between revisions
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== | |||
<StructureSection load='2x0h' size='340' side='right' caption='[[2x0h]], [[Resolution|resolution]] 2.21Å' scene=''> | ==BtGH84 Michaelis complex== | ||
<StructureSection load='2x0h' size='340' side='right'caption='[[2x0h]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2x0h]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2x0h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=14T:3,4-DIFLUOROPHENYL+2-DEOXY-2-[(DIFLUOROACETYL)AMINO]-BETA-D-GLUCOPYRANOSIDE'>14T</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=14T:3,4-DIFLUOROPHENYL+2-DEOXY-2-[(DIFLUOROACETYL)AMINO]-BETA-D-GLUCOPYRANOSIDE'>14T</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0h OCA], [https://pdbe.org/2x0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x0h RCSB], [https://www.ebi.ac.uk/pdbsum/2x0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0h ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/OGA_BACTN OGA_BACTN] 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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0h_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0h_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | ||
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | |||
*[[O-GlcNAcase|O-GlcNAcase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacteroides thetaiotaomicron VPI-5482]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Davies | [[Category: Davies GJ]] | ||
[[Category: He | [[Category: He Y]] | ||
Latest revision as of 13:21, 20 December 2023
BtGH84 Michaelis complexBtGH84 Michaelis complex
Structural highlights
FunctionOGA_BACTN 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 PubMedN-Acetylglucosamine beta-O-linked to serine and threonine residues of nucleocytoplasmic proteins (O-GlcNAc) has been linked to neurodegeneration, cellular stress response, and transcriptional regulation. Removal of O-GlcNAc is catalyzed by O-GlcNAcase (OGA) using a substrate-assisted catalytic mechanism. Here we define the reaction coordinate using chemical approaches and directly observe both a Michaelis complex and the oxazoline intermediate. Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase.,He Y, Macauley MS, Stubbs KA, Vocadlo DJ, Davies GJ J Am Chem Soc. 2010 Jan 12. PMID:20067256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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