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[[Image:2jal.gif|left|200px]]<br />
<applet load="2jal" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2jal, resolution 1.90&Aring;" />
'''BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH CYCLOPHELLITOL'''<br />


==Overview==
==Beta-glucosidase from Thermotoga maritima in complex with cyclophellitol==
The structural basis for beta-glucosidase inhibition by cyclophellitol is, demonstrated using X-ray crystallography, enzyme kinetics and mass, spectrometry.
<StructureSection load='2jal' size='340' side='right'caption='[[2jal]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</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/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.


==About this Structure==
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>
2JAL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with ACT, CA and YLL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: NUC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JAL OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17252125 17252125]
</div>
[[Category: Beta-glucosidase]]
<div class="pdbe-citations 2jal" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
 
==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[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: ACT]]
[[Category: CA]]
[[Category: YLL]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:28:37 2007''

Latest revision as of 12:13, 6 November 2024

Beta-glucosidase from Thermotoga maritima in complex with cyclophellitolBeta-glucosidase from Thermotoga maritima in complex with cyclophellitol

Structural highlights

2jal is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BGLA_THEMA

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

The structural basis for beta-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Gloster TM, Madsen R, Davies GJ. Structural basis for cyclophellitol inhibition of a beta-glucosidase. Org Biomol Chem. 2007 Feb 7;5(3):444-6. Epub 2006 Dec 14. PMID:17252125 doi:10.1039/b616590g

2jal, resolution 1.90Å

Drag the structure with the mouse to rotate

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