View source for 2jeq


==Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand==
<StructureSection load='2jeq' size='340' side='right'caption='[[2jeq]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jeq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_pabuli Paenibacillus pabuli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JEQ 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]] 1.94&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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=2jeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jeq OCA], [https://pdbe.org/2jeq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jeq RCSB], [https://www.ebi.ac.uk/pdbsum/2jeq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jeq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H9KVH3_9BACL H9KVH3_9BACL] 
== 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/je/2jeq_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=2jeq ConSurf].
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== Publication Abstract from PubMed ==
The plant cell wall is a complex material in which the cellulose microfibrils are embedded within a mesh of other polysaccharides, some of which are loosely termed "hemicellulose." One such hemicellulose is xyloglucan, which displays a beta-1,4-linked d-glucose backbone substituted with xylose, galactose, and occasionally fucose moieties. Both xyloglucan and the enzymes responsible for its modification and degradation are finding increasing prominence, reflecting both the drive for enzymatic biomass conversion, their role in detergent applications, and the utility of modified xyloglucans for cellulose fiber modification. Here we present the enzymatic characterization and three-dimensional structures in ligand-free and xyloglucan-oligosaccharide complexed forms of two distinct xyloglucanases from glycoside hydrolase families GH5 and GH12. The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (beta/alpha)(8) and beta-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated. For the beta-jelly roll enzyme topology of GH12, binding of xylosyl and pendant galactosyl moieties is tolerated, but the enzyme is similarly competent in the degradation of unbranched glucans. In the case of the (beta/alpha)(8) GH5 enzyme, kinetically productive interactions are made with both xylose and galactose substituents, as reflected in both a high specific activity on xyloglucan and the kinetics of a series of aryl glycosides. The differential strategies for the accommodation of the side chains of xyloglucan presumably facilitate the action of these microbial hydrolases in milieus where diverse and differently substituted substrates may be encountered.

Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12.,Gloster TM, Ibatullin FM, Macauley K, Eklof JM, Roberts S, Turkenburg JP, Bjornvad ME, Jorgensen PL, Danielsen S, Johansen KS, Borchert TV, Wilson KS, Brumer H, Davies GJ J Biol Chem. 2007 Jun 29;282(26):19177-89. Epub 2007 Mar 21. PMID:17376777<ref>PMID:17376777</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 2jeq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paenibacillus pabuli]]
[[Category: Bjornvad ME]]
[[Category: Borchert TV]]
[[Category: Brumer H]]
[[Category: Danielsen S]]
[[Category: Davies GJ]]
[[Category: Eklof JM]]
[[Category: Gloster TM]]
[[Category: Ibatullin FM]]
[[Category: Johansen K]]
[[Category: Jorgensen PL]]
[[Category: Macauley K]]
[[Category: Roberts S]]
[[Category: Turkenburg JP]]
[[Category: Wilson KS]]