6t8i

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m (Protected "6t8i" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6t8i is ON HOLD
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==Crystal structure of wild type EndoBT-3987 from Bacteroides thetaiotamicron VPI-5482==
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<StructureSection load='6t8i' size='340' side='right'caption='[[6t8i]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6t8i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T8I FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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=6t8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t8i OCA], [http://pdbe.org/6t8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t8i RCSB], [http://www.ebi.ac.uk/pdbsum/6t8i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t8i ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human gut microbiota plays a central role not only in regulating the metabolism of nutrients but also promoting immune homeostasis, immune responses and protection against pathogen colonization. The genome of the Gram-negative symbiont Bacteroides thetaiotaomicron, a dominant member of the human intestinal microbiota, encodes polysaccharide utilization loci PULs, the apparatus required to orchestrate the degradation of a specific glycan. EndoBT-3987 is a key endo-beta-N-acetylglucosaminidase (ENGase) that initiates the degradation/processing of mammalian high-mannose-type (HM-type) N-glycans in the intestine. Here, we provide structural snapshots of EndoBT-3987, including the unliganded form, the EndoBT-3987-Man9GlcNAc2Asn substrate complex, and two EndoBT-3987-Man9GlcNAc and EndoBT-3987-Man5GlcNAc product complexes. In combination with alanine scanning mutagenesis and activity measurements we unveil the molecular mechanism of HM-type recognition and specificity for EndoBT-3987 and an important group of the GH18 ENGases, including EndoH, an enzyme extensively used in biotechnology, and for which the mechanism of substrate recognition was largely unknown.
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Authors:
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Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides.,Trastoy B, Du JJ, Klontz EH, Li C, Cifuente JO, Wang LX, Sundberg EJ, Guerin ME Nat Commun. 2020 Feb 14;11(1):899. doi: 10.1038/s41467-020-14754-7. PMID:32060313<ref>PMID:32060313</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6t8i" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Cifuente, J O]]
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[[Category: Du, J J]]
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[[Category: Guerin, M E]]
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[[Category: Klontz, E H]]
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[[Category: Sundberg, E J]]
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[[Category: Trastoy, B]]
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[[Category: Endo-b-n-acetylglucosaminidase]]
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[[Category: Endobt]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]

Revision as of 09:24, 26 February 2020

Crystal structure of wild type EndoBT-3987 from Bacteroides thetaiotamicron VPI-5482

PDB ID 6t8i

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