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| | <StructureSection load='5noa' size='340' side='right'caption='[[5noa]], [[Resolution|resolution]] 1.26Å' scene=''> | | <StructureSection load='5noa' size='340' side='right'caption='[[5noa]], [[Resolution|resolution]] 1.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5noa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NOA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5noa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NOA FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unsaturated_rhamnogalacturonyl_hydrolase Unsaturated rhamnogalacturonyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.172 3.2.1.172] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.26Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5noa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5noa OCA], [http://pdbe.org/5noa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5noa RCSB], [http://www.ebi.ac.uk/pdbsum/5noa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5noa ProSAT]</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=5noa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5noa OCA], [https://pdbe.org/5noa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5noa RCSB], [https://www.ebi.ac.uk/pdbsum/5noa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5noa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8A1H4_BACTN Q8A1H4_BACTN] |
| | <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: Large Structures]] | |
| - | [[Category: Unsaturated rhamnogalacturonyl hydrolase]] | |
| - | [[Category: Basle, A]] | |
| - | [[Category: Cartmell, A]] | |
| - | [[Category: Gilbert, H J]] | |
| - | [[Category: Henrissat, B]] | |
| - | [[Category: Munoz-Munoz, J]] | |
| - | [[Category: Terrapon, N]] | |
| | [[Category: Bacteroides thetaiotaomicron]] | | [[Category: Bacteroides thetaiotaomicron]] |
| - | [[Category: Gum arabic]] | + | [[Category: Large Structures]] |
| - | [[Category: Human gut microbiota]] | + | [[Category: Basle A]] |
| - | [[Category: Hydrolase]] | + | [[Category: Cartmell A]] |
| - | [[Category: Polysaccharide lyase]] | + | [[Category: Gilbert HJ]] |
| | + | [[Category: Henrissat B]] |
| | + | [[Category: Munoz-Munoz J]] |
| | + | [[Category: Terrapon N]] |
| Structural highlights
Function
Q8A1H4_BACTN
Publication Abstract from PubMed
The human gut microbiota utilizes complex carbohydrates as major nutrients. The requirement for efficient glycan degrading systems exerts a major selection pressure on this microbial community. Thus, we propose that this microbial ecosystem represents a substantial resource for discovering novel carbohydrate active enzymes. To test this hypothesis we screened the potential enzymatic functions of hypothetical proteins encoded by genes of Bacteroides thetaiotaomicron that were up-regulated by arabinogalactan proteins or AGPs. Although AGPs are ubiquitous in plants, there is a paucity of information on their detailed structure, the function of these glycans in planta, and the mechanisms by which they are depolymerized in microbial ecosystems. Here we have discovered a new polysaccharide lyase family that is specific for the l-rhamnose-alpha1,4-d-glucuronic acid linkage that caps the side chains of complex AGPs. The reaction product generated by the lyase, Delta4,5-unsaturated uronic acid, is removed from AGP by a glycoside hydrolase located in family GH105, producing the final product 4-deoxy-beta-l-threo-hex-4-enepyranosyl-uronic acid. The crystal structure of a member of the novel lyase family revealed a catalytic domain that displays an (alpha/alpha)6 barrel-fold. In the center of the barrel is a deep pocket, which, based on mutagenesis data and amino acid conservation, comprises the active site of the lyase. A tyrosine is the proposed catalytic base in the beta-elimination reaction. This study illustrates how highly complex glycans can be used as a scaffold to discover new enzyme families within microbial ecosystems where carbohydrate metabolism is a major evolutionary driver.
An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins.,Munoz-Munoz J, Cartmell A, Terrapon N, Basle A, Henrissat B, Gilbert HJ J Biol Chem. 2017 Aug 11;292(32):13271-13283. doi: 10.1074/jbc.M117.794578. Epub , 2017 Jun 21. PMID:28637865[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Munoz-Munoz J, Cartmell A, Terrapon N, Basle A, Henrissat B, Gilbert HJ. An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins. J Biol Chem. 2017 Aug 11;292(32):13271-13283. doi: 10.1074/jbc.M117.794578. Epub , 2017 Jun 21. PMID:28637865 doi:http://dx.doi.org/10.1074/jbc.M117.794578
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