View source for 2wbg


==Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-castanospermine==
<StructureSection load='2wbg' size='340' side='right'caption='[[2wbg]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wbg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WBG 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]] 1.85&#8491;</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=LGS:(3Z,5S,6R,7S,8R,8AR)-3-(OCTYLIMINO)HEXAHYDRO[1,3]OXAZOLO[3,4-A]PYRIDINE-5,6,7,8-TETROL'>LGS</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=2wbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbg OCA], [https://pdbe.org/2wbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wbg RCSB], [https://www.ebi.ac.uk/pdbsum/2wbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wbg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BGLA_THEMA BGLA_THEMA] 
== 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/wb/2wbg_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=2wbg ConSurf].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2wbg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Aguilar M]]
[[Category: Davies GJ]]
[[Category: Garcia Fernandez JM]]
[[Category: Garcia-Moreno MI]]
[[Category: Gloster TM]]
[[Category: Ortiz Mellet C]]
[[Category: Turkenburg JP]]