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==Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium== | ==Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium== | ||
<StructureSection load='7l1w' size='340' side='right'caption='[[7l1w]]' scene=''> | <StructureSection load='7l1w' size='340' side='right'caption='[[7l1w]], [[Resolution|resolution]] 1.71Å' 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=7L1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L1W FirstGlance]. <br> | <table><tr><td colspan='2'>[[7l1w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L1W 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=7l1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l1w OCA], [https://pdbe.org/7l1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l1w RCSB], [https://www.ebi.ac.uk/pdbsum/7l1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l1w 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=7l1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l1w OCA], [https://pdbe.org/7l1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l1w RCSB], [https://www.ebi.ac.uk/pdbsum/7l1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l1w ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-beta-1,4-xylanases, beta-xylosidases, acetylxylan esterases, alpha-l-arabinofuranosidases, and alpha-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-beta-1,4- and beta-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase. | |||
Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium.,Kadowaki MAS, Briganti L, Evangelista DE, Echevarria-Poza A, Tryfona T, Pellegrini VOA, Nakayama DG, Dupree P, Polikarpov I Biotechnol Bioeng. 2021 Jul 7. doi: 10.1002/bit.27880. PMID:34232504<ref>PMID:34232504</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7l1w" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Briganti L]] | [[Category: Miscellaneous nucleic acid]] | ||
[[Category: Evangelista | [[Category: Briganti, L]] | ||
[[Category: Kadowaki | [[Category: Evangelista, D E]] | ||
[[Category: Polikarpov I]] | [[Category: Kadowaki, M A.S]] | ||
[[Category: Polikarpov, I]] | |||
[[Category: 4-xylobiosidase]] | |||
[[Category: Gh11 exo-b-1]] | |||
[[Category: Glycoside hydrolase family 11]] | |||
[[Category: Hydrolase]] | |||
Revision as of 10:00, 22 September 2021
Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortiumUnlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium
Structural highlights
Publication Abstract from PubMedThe heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-beta-1,4-xylanases, beta-xylosidases, acetylxylan esterases, alpha-l-arabinofuranosidases, and alpha-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-beta-1,4- and beta-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase. Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium.,Kadowaki MAS, Briganti L, Evangelista DE, Echevarria-Poza A, Tryfona T, Pellegrini VOA, Nakayama DG, Dupree P, Polikarpov I Biotechnol Bioeng. 2021 Jul 7. doi: 10.1002/bit.27880. PMID:34232504[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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