7p6g
From Proteopedia
(Difference between revisions)
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==Crystal structure of the endoglucanase RBcel1 E135Q== | ==Crystal structure of the endoglucanase RBcel1 E135Q== | ||
| - | <StructureSection load='7p6g' size='340' side='right'caption='[[7p6g]]' scene=''> | + | <StructureSection load='7p6g' size='340' side='right'caption='[[7p6g]], [[Resolution|resolution]] 1.49Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P6G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7p6g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P6G FirstGlance]. <br> |
| - | </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=7p6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p6g OCA], [https://pdbe.org/7p6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p6g RCSB], [https://www.ebi.ac.uk/pdbsum/7p6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p6g ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></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=7p6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p6g OCA], [https://pdbe.org/7p6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p6g RCSB], [https://www.ebi.ac.uk/pdbsum/7p6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p6g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transglycosylating glycoside hydrolases (GHs) offer great potential for the enzymatic synthesis of oligosaccharides. Although knowledge is progressing, there is no unique strategy to improve the transglycosylation yield. Obtaining efficient enzymatic tools for glycan synthesis with GHs remains dependent on an improved understanding of the molecular factors governing the balance between hydrolysis and transglycosylation. This enzymatic and structural study of RBcel1, a transglycosylase from the GH5_5 subfamily isolated from an uncultured bacterium, aims to unravel such factors. The size of the acceptor and donor sugars was found to be critical since transglycosylation is efficient with oligosaccharides at least the size of cellotetraose as the donor and cellotriose as the acceptor. The reaction pH is important in driving the balance between hydrolysis and transglycosylation: hydrolysis is favored at pH values below 8, while transglycosylation becomes the major reaction at basic pH. Solving the structures of two RBcel1 variants, RBcel1_E135Q and RBcel1_Y201F, in complex with ligands has brought to light some of the molecular factors behind transglycosylation. The structure of RBcel1_E135Q in complex with cellotriose allowed a +3 subsite to be defined, in accordance with the requirement for cellotriose as a transglycosylation acceptor. The structure of RBcel1_Y201F has been obtained with several transglycosylation intermediates, providing crystallographic evidence of transglycosylation. The catalytic cleft is filled with (i) donors ranging from cellotriose to cellohexaose in the negative subsites and (ii) cellobiose and cellotriose in the positive subsites. Such a structure is particularly relevant since it is the first structure of a GH5 enzyme in complex with transglycosylation products that has been obtained with neither of the catalytic glutamate residues modified. | ||
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| + | Highlighting the factors governing transglycosylation in the GH5_5 endo-1,4-beta-glucanase RBcel1.,Collet L, Vander Wauven C, Oudjama Y, Galleni M, Dutoit R Acta Crystallogr D Struct Biol. 2022 Mar 1;78(Pt 3):278-289. doi:, 10.1107/S2059798321013541. Epub 2022 Feb 18. PMID:35234142<ref>PMID:35234142</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7p6g" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Cellulase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Collet L]] | + | [[Category: Collet, L]] |
| - | [[Category: Dutoit R]] | + | [[Category: Dutoit, R]] |
| + | [[Category: Gh5_5 family]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Transglycosylase]] | ||
Revision as of 07:18, 16 March 2022
Crystal structure of the endoglucanase RBcel1 E135Q
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