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2wc4
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine== |
| + | <StructureSection load='2wc4' size='340' side='right' caption='[[2wc4]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2wc4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WC4 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AMF:(3Z,5S,6R,7S,8R,8AS)-3-(OCTYLIMINO)HEXAHYDRO[1,3]THIAZOLO[3,4-A]PYRIDINE-5,6,7,8-TETROL'>AMF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wc3|2wc3]], [[1w3j|1w3j]], [[2j78|2j78]], [[2j75|2j75]], [[2j7g|2j7g]], [[2jal|2jal]], [[2vrj|2vrj]], [[2j7e|2j7e]], [[2cbu|2cbu]], [[2j7h|2j7h]], [[1oin|1oin]], [[2j7c|2j7c]], [[2cet|2cet]], [[1oif|1oif]], [[2j79|2j79]], [[2j7b|2j7b]], [[1uz1|1uz1]], [[1od0|1od0]], [[2ces|2ces]], [[2j7d|2j7d]], [[2j7f|2j7f]], [[2wbg|2wbg]], [[1oim|1oim]], [[2j77|2j77]], [[2cbv|2cbv]]</td></tr> | ||
| + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wc4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wc4 RCSB], [http://www.ebi.ac.uk/pdbsum/2wc4 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == 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/wc/2wc4_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Synthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase. | ||
| - | + | Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.,Aguilar-Moncayo M, Gloster TM, Turkenburg JP, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Garcia Fernandez JM Org Biomol Chem. 2009 Jul 7;7(13):2738-47. Epub 2009 May 22. PMID:19532990<ref>PMID:19532990</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Beta-glucosidase|Beta-glucosidase]] | *[[Beta-glucosidase|Beta-glucosidase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
Revision as of 10:21, 29 September 2014
Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine
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Categories: Beta-glucosidase | Thermotoga maritima | Aguilar, M. | Davies, G J. | Fernandez, J M.Garcia. | Garcia-Moreno, M I. | Gloster, T M. | Mellet, C Ortiz. | Turkenburg, J P. | Carbohydrate metabolism | Castanospermine | Cellulose degradation | Family 1 | Glycosidase | Glycoside hydrolase | Hydrolase | Inhibitor | Polysaccharide degradation
