5oss: Difference between revisions
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==Beta-glucosidase from Thermotoga maritima in complex with Gluco-1H-imidazole== | ==Beta-glucosidase from Thermotoga maritima in complex with Gluco-1H-imidazole== | ||
<StructureSection load='5oss' size='340' side='right' caption='[[5oss]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5oss' size='340' side='right'caption='[[5oss]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oss]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OSS OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5oss]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OSS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OSS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AEZ:(4~{S},5~{S},6~{R},7~{R})-7-(hydroxymethyl)-4,5,6,7-tetrahydro-1~{H}-benzimidazole-4,5,6-triol'>AEZ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AEZ:(4~{S},5~{S},6~{R},7~{R})-7-(hydroxymethyl)-4,5,6,7-tetrahydro-1~{H}-benzimidazole-4,5,6-triol'>AEZ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5oss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oss OCA], [http://pdbe.org/5oss PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oss RCSB], [http://www.ebi.ac.uk/pdbsum/5oss PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oss ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5oss" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5oss" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Large Structures]] | |||
[[Category: Davies, G J]] | [[Category: Davies, G J]] | ||
[[Category: Offen, W A]] | [[Category: Offen, W A]] | ||
Revision as of 10:31, 2 September 2020
Beta-glucosidase from Thermotoga maritima in complex with Gluco-1H-imidazoleBeta-glucosidase from Thermotoga maritima in complex with Gluco-1H-imidazole
Structural highlights
Publication Abstract from PubMedGluco-azoles competitively inhibit glucosidases by transition-state mimicry and their ability to interact with catalytic acid residues in glucosidase active sites. We noted that no azole-type inhibitors described, to date, possess a protic nitrogen characteristic for 1 H-imidazoles. Here, we present gluco-1 H-imidazole, a gluco-azole bearing a 1 H-imidazole fused to a glucopyranose-configured cyclitol core, and three close analogues as new glucosidase inhibitors. All compounds inhibit human retaining beta-glucosidase, GBA1, with the most potent ones inhibiting this enzyme (deficient in Gaucher disease) on a par with glucoimidazole. None inhibit glucosylceramide synthase, cytosolic beta-glucosidase GBA2 or alpha-glucosidase GAA. Structural, physical and computational studies provide first insights into the binding mode of this conceptually new class of retaining beta-glucosidase inhibitors. Gluco-1 H-imidazole: A New Class of Azole-Type beta-Glucosidase Inhibitor.,Schroder SP, Wu L, Artola M, Hansen T, Offen WA, Ferraz MJ, Li KY, Aerts JMFG, van der Marel GA, Codee JDC, Davies GJ, Overkleeft HS J Am Chem Soc. 2018 Apr 4. doi: 10.1021/jacs.8b02399. PMID:29601200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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