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| | <StructureSection load='4d1i' size='340' side='right'caption='[[4d1i]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4d1i' size='340' side='right'caption='[[4d1i]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d1i]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D1I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d1i]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus_Ueda107 Cellvibrio japonicus Ueda107]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D1I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d1j|4d1j]]</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=4d1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d1i OCA], [https://pdbe.org/4d1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d1i RCSB], [https://www.ebi.ac.uk/pdbsum/4d1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d1i ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d1i OCA], [http://pdbe.org/4d1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d1i RCSB], [http://www.ebi.ac.uk/pdbsum/4d1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d1i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/B3PBE0_CELJU B3PBE0_CELJU]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-galactosidase]] | + | [[Category: Cellvibrio japonicus Ueda107]] |
| - | [[Category: Celju]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brumer, H]] | + | [[Category: Brumer H]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Gardner, J G]] | + | [[Category: Gardner JG]] |
| - | [[Category: Larsbrink, J]] | + | [[Category: Larsbrink J]] |
| - | [[Category: Lundqvist, M]] | + | [[Category: Lundqvist M]] |
| - | [[Category: Thompson, A J]] | + | [[Category: Thompson AJ]] |
| - | [[Category: Enzyme-carbohydrate interaction]]
| + | |
| - | [[Category: Glycosidase inhibition]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
[B3PBE0_CELJU]
Publication Abstract from PubMed
The degradation of plant biomass by saprophytes is an ecologically important part of the global carbon cycle, which has also inspired a vast diversity of industrial enzyme applications. The xyloglucans (XyGs) constitute a family of ubiquitous and abundant plant cell wall polysaccharides, yet the enzymology of XyG saccharification is poorly studied. Here, we present the identification and molecular characterization of a complex genetic locus that is required for xyloglucan utilization by the model saprophyte Cellvibrio japonicus. In harness, transcriptomics, reverse genetics, enzyme kinetics, and structural biology indicate that the encoded cohort of an alpha-xylosidase, a beta-galactosidase, and an alpha-l-fucosidase is specifically adapted for efficient, concerted saccharification of dicot (fucogalacto)xyloglucan oligosaccharides following import into the periplasm via an associated TonB-dependent receptor. The data support a biological model of xyloglucan degradation by C. japonicus with striking similarities - and notable differences - to the complex polysaccharide utilization loci of the Bacteroidetes.
A complex gene locus enables xyloglucan utilization in the model saprophyte Cellvibrio japonicus.,Larsbrink J, Thompson AJ, Lundqvist M, Gardner JG, Davies GJ, Brumer H Mol Microbiol. 2014 Oct;94(2):418-33. doi: 10.1111/mmi.12776. Epub 2014 Sep 17. PMID:25171165[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Larsbrink J, Thompson AJ, Lundqvist M, Gardner JG, Davies GJ, Brumer H. A complex gene locus enables xyloglucan utilization in the model saprophyte Cellvibrio japonicus. Mol Microbiol. 2014 Oct;94(2):418-33. doi: 10.1111/mmi.12776. Epub 2014 Sep 17. PMID:25171165 doi:http://dx.doi.org/10.1111/mmi.12776
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