2jal: Difference between revisions

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[[Image:2jal.gif|left|200px]]


{{Structure
==Beta-glucosidase from Thermotoga maritima in complex with cyclophellitol==
|PDB= 2jal |SIZE=350|CAPTION= <scene name='initialview01'>2jal</scene>, resolution 1.90&Aring;
<StructureSection load='2jal' size='340' side='right'caption='[[2jal]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=NUC:Ca+Binding+Site+For+Chain+B'>NUC</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YLL:(1R,2S,3S,4S,5R,6R)-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4,5-PENTOL'>YLL</scene>
<table><tr><td colspan='2'>[[2jal]] is a 2 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=2JAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAL FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=
<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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YLL:(1R,2S,3S,4S,5R,6R)-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4,5-PENTOL'>YLL</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jal OCA], [https://pdbe.org/2jal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jal RCSB], [https://www.ebi.ac.uk/pdbsum/2jal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jal ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jal OCA], [http://www.ebi.ac.uk/pdbsum/2jal PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jal RCSB]</span>
== 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/ja/2jal_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2jal ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structural basis for beta-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry.


'''BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH CYCLOPHELLITOL'''
Structural basis for cyclophellitol inhibition of a beta-glucosidase.,Gloster TM, Madsen R, Davies GJ Org Biomol Chem. 2007 Feb 7;5(3):444-6. Epub 2006 Dec 14. PMID:17252125<ref>PMID:17252125</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jal" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The structural basis for beta-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry.
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2JAL is a [[Single protein]] structure of 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=2JAL OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structural basis for cyclophellitol inhibition of a beta-glucosidase., Gloster TM, Madsen R, Davies GJ, Org Biomol Chem. 2007 Feb 7;5(3):444-6. Epub 2006 Dec 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17252125 17252125]
[[Category: Beta-glucosidase]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Davies, G J.]]
[[Category: Davies GJ]]
[[Category: Gloster, T M.]]
[[Category: Gloster TM]]
[[Category: Madsen, R.]]
[[Category: Madsen R]]
[[Category: carbohydrate metabolism]]
[[Category: cellulose degradation]]
[[Category: covalent]]
[[Category: family 1]]
[[Category: glycosidase]]
[[Category: glycoside hydrolase]]
[[Category: hydrolase]]
[[Category: inhibitor]]
[[Category: polysaccharide degradation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:25 2008''
Retrieved from "https://proteopedia.org/2jal"