3d6e

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[[Image:3d6e.png|left|200px]]
 
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==Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis==
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The line below this paragraph, containing "STRUCTURE_3d6e", creates the "Structure Box" on the page.
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<StructureSection load='3d6e' size='340' side='right'caption='[[3d6e]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3d6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D6E FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_3d6e| PDB=3d6e | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d6e OCA], [https://pdbe.org/3d6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d6e RCSB], [https://www.ebi.ac.uk/pdbsum/3d6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d6e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUB_BACLI GUB_BACLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/3d6e_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3d6e ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Family 16 carbohydrate active enzyme members Bacillus licheniformis 1,3-1,4-beta-glucanase and Populus tremula x tremuloides xyloglucan endotransglycosylase (XET16-34) are highly structurally related but display different substrate specificities. Although the first binds linear gluco-oligosaccharides, the second binds branched xylogluco-oligosaccharides. Prior engineered nucleophile mutants of both enzymes are glycosynthases that catalyze the condensation between a glycosyl fluoride donor and a glycoside acceptor. With the aim of expanding the glycosynthase technology to produce designer oligosaccharides consisting of hybrids between branched xylogluco- and linear gluco-oligosaccharides, enzyme engineering on the negative subsites of 1,3-1,4-beta-glucanase to accept branched substrates has been undertaken. Removal of the 1,3-1,4-beta-glucanase major loop and replacement with that of XET16-34 to open the binding cleft resulted in a folded protein, which still maintained some beta-glucan hydrolase activity, but the corresponding nucleophile mutant did not display glycosynthase activity with either linear or branched glycosyl donors. Next, point mutations of the 1,3-1,4-beta-glucanase beta-sheets forming the binding site cleft were mutated to resemble XET16-34 residues. The final chimeric protein acquired binding affinity for xyloglucan and did not bind beta-glucan. Therefore, binding specificity has been re-engineered, but affinity was low and the nucleophile mutant of the chimeric enzyme did not show glycosynthase activity to produce the target hybrid oligosaccharides. Structural analysis by X-ray crystallography explains these results in terms of changes in the protein structure and highlights further engineering approaches toward introducing the desired activity. Proteins 2010. (c) 2010 Wiley-Liss, Inc.
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===Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis===
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Re-engineering specificity in 1,3-1, 4-beta-glucanase to accept branched xyloglucan substrates.,Addington T, Calisto B, Alfonso-Prieto M, Rovira C, Fita I, Planas A Proteins. 2010 Sep 22. PMID:21069723<ref>PMID:21069723</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3d6e" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21069723}}, adds the Publication Abstract to the page
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21069723 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21069723}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3d6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D6E OCA].
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==Reference==
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<ref group="xtra">PMID:21069723</ref><ref group="xtra">PMID:7589539</ref><references group="xtra"/>
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[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
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[[Category: Licheninase]]
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[[Category: Large Structures]]
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[[Category: Addington, T.]]
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[[Category: Addington T]]
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[[Category: Calisto, B M.]]
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[[Category: Calisto BM]]
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[[Category: Fita, I.]]
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[[Category: Fita I]]
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[[Category: Planas, A.]]
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[[Category: Planas A]]

Current revision

Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis

PDB ID 3d6e

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