6euf: Difference between revisions
New page: '''Unreleased structure''' The entry 6euf is ON HOLD Authors: Cartmell, A., Gilbert, H.J. Description: The GH43, Beta 1,3 Glacatosidase, BT0265 Category: Unreleased Structures [[Ca... |
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The | ==The GH43, Beta 1,3 Galactosidase, BT0265== | ||
<StructureSection load='6euf' size='340' side='right'caption='[[6euf]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6euf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EUF 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</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=6euf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6euf OCA], [https://pdbe.org/6euf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6euf RCSB], [https://www.ebi.ac.uk/pdbsum/6euf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6euf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8AB46_BACTN Q8AB46_BACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glycans are major nutrients for the human gut microbiota (HGM). Arabinogalactan proteins (AGPs) comprise a heterogenous group of plant glycans in which a beta1,3-galactan backbone and beta1,6-galactan side chains are conserved. Diversity is provided by the variable nature of the sugars that decorate the galactans. The mechanisms by which nutritionally relevant AGPs are degraded in the HGM are poorly understood. Here we explore how the HGM organism Bacteroides thetaiotaomicron metabolizes AGPs. We propose a sequential degradative model in which exo-acting glycoside hydrolase (GH) family 43 beta1,3-galactanases release the side chains. These oligosaccharide side chains are depolymerized by the synergistic action of exo-acting enzymes in which catalytic interactions are dependent on whether degradation is initiated by a lyase or GH. We identified two GHs that establish two previously undiscovered GH families. The crystal structures of the exo-beta1,3-galactanases identified a key specificity determinant and departure from the canonical catalytic apparatus of GH43 enzymes. Growth studies of Bacteroidetes spp. on complex AGP revealed 3 keystone organisms that facilitated utilization of the glycan by 17 recipient bacteria, which included B. thetaiotaomicron. A surface endo-beta1,3-galactanase, when engineered into B. thetaiotaomicron, enabled the bacterium to utilize complex AGPs and act as a keystone organism. | |||
A surface endogalactanase in Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation.,Cartmell A, Munoz-Munoz J, Briggs JA, Ndeh DA, Lowe EC, Basle A, Terrapon N, Stott K, Heunis T, Gray J, Yu L, Dupree P, Fernandes PZ, Shah S, Williams SJ, Labourel A, Trost M, Henrissat B, Gilbert HJ Nat Microbiol. 2018 Nov;3(11):1314-1326. doi: 10.1038/s41564-018-0258-8. Epub, 2018 Oct 22. PMID:30349080<ref>PMID:30349080</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Cartmell | <div class="pdbe-citations 6euf" style="background-color:#fffaf0;"></div> | ||
[[Category: Gilbert | |||
==See Also== | |||
*[[Galactosidase 3D structures|Galactosidase 3D structures]] | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteroides thetaiotaomicron VPI-5482]] | |||
[[Category: Large Structures]] | |||
[[Category: Cartmell A]] | |||
[[Category: Gilbert HJ]] | |||
Latest revision as of 15:21, 9 May 2024
The GH43, Beta 1,3 Galactosidase, BT0265The GH43, Beta 1,3 Galactosidase, BT0265
Structural highlights
FunctionPublication Abstract from PubMedGlycans are major nutrients for the human gut microbiota (HGM). Arabinogalactan proteins (AGPs) comprise a heterogenous group of plant glycans in which a beta1,3-galactan backbone and beta1,6-galactan side chains are conserved. Diversity is provided by the variable nature of the sugars that decorate the galactans. The mechanisms by which nutritionally relevant AGPs are degraded in the HGM are poorly understood. Here we explore how the HGM organism Bacteroides thetaiotaomicron metabolizes AGPs. We propose a sequential degradative model in which exo-acting glycoside hydrolase (GH) family 43 beta1,3-galactanases release the side chains. These oligosaccharide side chains are depolymerized by the synergistic action of exo-acting enzymes in which catalytic interactions are dependent on whether degradation is initiated by a lyase or GH. We identified two GHs that establish two previously undiscovered GH families. The crystal structures of the exo-beta1,3-galactanases identified a key specificity determinant and departure from the canonical catalytic apparatus of GH43 enzymes. Growth studies of Bacteroidetes spp. on complex AGP revealed 3 keystone organisms that facilitated utilization of the glycan by 17 recipient bacteria, which included B. thetaiotaomicron. A surface endo-beta1,3-galactanase, when engineered into B. thetaiotaomicron, enabled the bacterium to utilize complex AGPs and act as a keystone organism. A surface endogalactanase in Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation.,Cartmell A, Munoz-Munoz J, Briggs JA, Ndeh DA, Lowe EC, Basle A, Terrapon N, Stott K, Heunis T, Gray J, Yu L, Dupree P, Fernandes PZ, Shah S, Williams SJ, Labourel A, Trost M, Henrissat B, Gilbert HJ Nat Microbiol. 2018 Nov;3(11):1314-1326. doi: 10.1038/s41564-018-0258-8. Epub, 2018 Oct 22. PMID:30349080[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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