|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Beta-glycosidase from Sulfolobus solfataricus in complex with glucoimidazole== | | ==Beta-glycosidase from Sulfolobus solfataricus in complex with glucoimidazole== |
| - | <StructureSection load='2ceq' size='340' side='right' caption='[[2ceq]], [[Resolution|resolution]] 2.14Å' scene=''> | + | <StructureSection load='2ceq' size='340' side='right'caption='[[2ceq]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ceq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CEQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ceq]] 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=2CEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CEQ 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=GIM:GLUCOIMIDAZOLE'>GIM</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]] 2.14Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gow|1gow]], [[1uwi|1uwi]], [[1uwq|1uwq]], [[1uwr|1uwr]], [[1uws|1uws]], [[1uwt|1uwt]], [[1uwu|1uwu]], [[2cer|2cer]]</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=GIM:GLUCOIMIDAZOLE'>GIM</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-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=2ceq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ceq OCA], [https://pdbe.org/2ceq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ceq RCSB], [https://www.ebi.ac.uk/pdbsum/2ceq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ceq ProSAT]</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=2ceq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ceq OCA], [http://pdbe.org/2ceq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ceq RCSB], [http://www.ebi.ac.uk/pdbsum/2ceq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ceq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BGAL_SACS2 BGAL_SACS2] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Galactosidase|Galactosidase]] | + | *[[Galactosidase 3D structures|Galactosidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Saccharolobus solfataricus]] | | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Beta-galactosidase]]
| + | [[Category: Davies GJ]] |
| - | [[Category: Davies, G J]] | + | [[Category: Gloster TM]] |
| - | [[Category: Gloster, T M]] | + | [[Category: Moracci M]] |
| - | [[Category: Moracci, M]] | + | [[Category: Vasella A]] |
| - | [[Category: Vasella, A]] | + | |
| - | [[Category: Archaeon]]
| + | |
| - | [[Category: Family 1]]
| + | |
| - | [[Category: Glucoimidazole]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
BGAL_SACS2
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
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gloster TM, Roberts S, Perugino G, Rossi M, Moracci M, Panday N, Terinek M, Vasella A, Davies GJ. Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors. Biochemistry. 2006 Oct 3;45(39):11879-84. PMID:17002288 doi:10.1021/bi060973x
|
