2cet: Difference between revisions
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<StructureSection load='2cet' size='340' side='right' caption='[[2cet]], [[Resolution|resolution]] 1.97Å' scene=''> | <StructureSection load='2cet' size='340' side='right' caption='[[2cet]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cet]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2cet]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CET FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1od0|1od0]], [[1oif|1oif]], [[1oim|1oim]], [[1oin|1oin]], [[1uz1|1uz1]], [[1w3j|1w3j]], [[2cbu|2cbu]], [[2cbv|2cbv]], [[2ces|2ces]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1od0|1od0]], [[1oif|1oif]], [[1oim|1oim]], [[1oin|1oin]], [[1uz1|1uz1]], [[1w3j|1w3j]], [[2cbu|2cbu]], [[2cbv|2cbv]], [[2ces|2ces]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cet OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cet RCSB], [http://www.ebi.ac.uk/pdbsum/2cet PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cet OCA], [http://pdbe.org/2cet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cet RCSB], [http://www.ebi.ac.uk/pdbsum/2cet PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2cet" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43589]] | |||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Davies, G J]] | [[Category: Davies, G J]] | ||
[[Category: Gloster, T M]] | [[Category: Gloster, T M]] | ||
Revision as of 02:09, 12 September 2015
BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH PHENETHYL-SUBSTITUTED GLUCOIMIDAZOLEBETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH PHENETHYL-SUBSTITUTED GLUCOIMIDAZOLE
Structural highlights
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 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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