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New page: left|200px<br /> <applet load="2cer" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cer, resolution 2.29Å" /> '''BETA-GLYCOSIDASE FR... |
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== | ==Beta-glycosidase from Sulfolobus solfataricus in complex with phenethyl-substituted glucoimidazole== | ||
Inhibition of glycosidases has great potential in the quest for highly | <StructureSection load='2cer' size='340' side='right'caption='[[2cer]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2cer]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CER FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PGI:(5R,6R,7S,8S)-5-(HYDROXYMETHYL)-2-(2-PHENYLETHYL)-1,5,6,7,8,8A-HEXAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL'>PGI</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=2cer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cer OCA], [https://pdbe.org/2cer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cer RCSB], [https://www.ebi.ac.uk/pdbsum/2cer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cer ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BGAL_SACS2 BGAL_SACS2] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/2cer_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cer ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Inhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound. | |||
Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors.,Gloster TM, Roberts S, Perugino G, Rossi M, Moracci M, Panday N, Terinek M, Vasella A, Davies GJ Biochemistry. 2006 Oct 3;45(39):11879-84. PMID:17002288<ref>PMID:17002288</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2cer" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
*[[Galactosidase 3D structures|Galactosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharolobus solfataricus]] | |||
[[Category: Davies GJ]] | |||
[[Category: Gloster TM]] | |||
[[Category: Moracci M]] | |||
[[Category: Roberts S]] | |||
[[Category: Vasella A]] | |||
Latest revision as of 17:15, 13 December 2023
Beta-glycosidase from Sulfolobus solfataricus in complex with phenethyl-substituted glucoimidazoleBeta-glycosidase from Sulfolobus solfataricus in complex with phenethyl-substituted glucoimidazole
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound. Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors.,Gloster TM, Roberts S, Perugino G, Rossi M, Moracci M, Panday N, Terinek M, Vasella A, Davies GJ Biochemistry. 2006 Oct 3;45(39):11879-84. PMID:17002288[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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