View source for 7zgn


==Plant/insect N-glycan active PNGase==
<StructureSection load='7zgn' size='340' side='right'caption='[[7zgn]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zgn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phocaeicola_massiliensis_B84634_=_Timone_84634_=_DSM_17679_=_JCM_13223 Phocaeicola massiliensis B84634 = Timone 84634 = DSM 17679 = JCM 13223]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZGN 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]] 1.95&#8491;</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=7zgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zgn OCA], [https://pdbe.org/7zgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zgn RCSB], [https://www.ebi.ac.uk/pdbsum/7zgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zgn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U6RE59_9BACT U6RE59_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The major nutrients available to the human colonic microbiota are complex glycans derived from the diet. To degrade this highly variable mix of sugar structures, gut microbes have acquired a huge array of different carbohydrate-active enzymes (CAZymes), predominantly glycoside hydrolases, many of which have specificities that can be exploited for a range of different applications. Plant N-glycans are prevalent on proteins produced by plants and thus components of the diet, but the breakdown of these complex molecules by the gut microbiota has not been explored. Plant N-glycans are also well characterized allergens in pollen and some plant-based foods, and when plants are used in heterologous protein production for medical applications, the N-glycans present can pose a risk to therapeutic function and stability. Here we use a novel genome association approach for enzyme discovery to identify a breakdown pathway for plant complex N-glycans encoded by a gut Bacteroides species and biochemically characterize five CAZymes involved, including structures of the PNGase and GH92 alpha-mannosidase. These enzymes provide a toolbox for the modification of plant N-glycans for a range of potential applications. Furthermore, the keystone PNGase also has activity against insect-type N-glycans, which we discuss from the perspective of insects as a nutrient source.

Plant N-glycan breakdown by human gut Bacteroides.,Crouch LI, Urbanowicz PA, Basle A, Cai ZP, Liu L, Voglmeir J, Melo Diaz JM, Benedict ST, Spencer DIR, Bolam DN Proc Natl Acad Sci U S A. 2022 Sep 27;119(39):e2208168119. doi: , 10.1073/pnas.2208168119. Epub 2022 Sep 19. PMID:36122227<ref>PMID:36122227</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7zgn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phocaeicola massiliensis B84634 = Timone 84634 = DSM 17679 = JCM 13223]]
[[Category: Basle A]]
[[Category: Bolam D]]
[[Category: Crouch L]]