View source for 7bvr


==DgpB-DgpC complex apo==
<StructureSection load='7bvr' size='340' side='right'caption='[[7bvr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bvr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_intestinal_bacterium_PUE Human intestinal bacterium PUE]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BVR 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=7bvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bvr OCA], [https://pdbe.org/7bvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bvr RCSB], [https://www.ebi.ac.uk/pdbsum/7bvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bvr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3Q9WXL1_9BACT A0A3Q9WXL1_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
C-Glycosides, in which a sugar moiety is linked via a carbon-carbon (C-C) bond to a non-sugar moiety (aglycone), are found in our food and medicine. The C-C bond is cleaved by intestinal microbes and the resulting aglycones exert various bioactivities. Although the enzymes responsible for the reactions have been identified, their catalytic mechanisms and the generality of the reactions in nature remain to be explored. Here, we present the identification and structural basis for the activation of xenobiotic C-glycosides by heterocomplex C-deglycosylation enzymes from intestinal and soil bacteria. They are found to be metal-dependent enzymes exhibiting broad substrate specificity toward C-glycosides. X-ray crystallographic and cryo-electron microscopic analyses, as well as structure-based mutagenesis, reveal the structural details of these enzymes and the detailed catalytic mechanisms of their remarkable C-C bond cleavage reactions. Furthermore, bioinformatic and biochemical analyses suggest that the C-deglycosylation enzymes are widely distributed in the gut, soil, and marine bacteria.

C-Glycoside metabolism in the gut and in nature: Identification, characterization, structural analyses and distribution of C-C bond-cleaving enzymes.,Mori T, Kumano T, He H, Watanabe S, Senda M, Moriya T, Adachi N, Hori S, Terashita Y, Kawasaki M, Hashimoto Y, Awakawa T, Senda T, Abe I, Kobayashi M Nat Commun. 2021 Nov 2;12(1):6294. doi: 10.1038/s41467-021-26585-1. PMID:34728636<ref>PMID:34728636</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bvr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human intestinal bacterium PUE]]
[[Category: Large Structures]]
[[Category: Abe I]]
[[Category: He H]]
[[Category: Mori T]]