6rtg
From Proteopedia
(Difference between revisions)
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<StructureSection load='6rtg' size='340' side='right'caption='[[6rtg]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6rtg' size='340' side='right'caption='[[6rtg]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6rtg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RTG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rtg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yermw Yermw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RTG FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ymoll0001_37990 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=349967 YERMW])</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=6rtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rtg OCA], [http://pdbe.org/6rtg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rtg RCSB], [http://www.ebi.ac.uk/pdbsum/6rtg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rtg ProSAT]</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=6rtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rtg OCA], [http://pdbe.org/6rtg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rtg RCSB], [http://www.ebi.ac.uk/pdbsum/6rtg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rtg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We identified a glucosyltransferase (YGT) and an ADP-ribosyltransferase (YART) in Yersinia mollaretii, highly related to glucosylating toxins from Clostridium difficile, the cause of antibiotics-associated enterocolitis. Both Yersinia toxins consist of an amino-terminal enzyme domain, an autoprotease domain activated by inositol hexakisphosphate, and a carboxyl-terminal translocation domain. YGT N-acetylglucosaminylates Rab5 and Rab31 at Thr(52) and Thr(36), respectively, thereby inactivating the Rab proteins. YART ADP-ribosylates Rab5 and Rab31 at Gln(79) and Gln(64), respectively. This activates Rab proteins by inhibiting GTP hydrolysis. We determined the crystal structure of the glycosyltransferase domain of YGT (YGT(G)) in the presence and absence of UDP at 1.9- and 3.4-A resolution, respectively. Thereby, we identified a previously unknown potassium ion-binding site, which explains potassium ion-dependent enhanced glycosyltransferase activity in clostridial and related toxins. Our findings exhibit a novel type of inverse regulation of Rab proteins by toxins and provide new insights into the structure-function relationship of glycosyltransferase toxins. | ||
| + | |||
| + | Inverse control of Rab proteins by Yersinia ADP-ribosyltransferase and glycosyltransferase related to clostridial glucosylating toxins.,Ost GS, Wirth C, Bogdanovic X, Kao WC, Schorch B, Aktories PJK, Papatheodorou P, Schwan C, Schlosser A, Jank T, Hunte C, Aktories K Sci Adv. 2020 Mar 11;6(11):eaaz2094. doi: 10.1126/sciadv.aaz2094. eCollection, 2020 Mar. PMID:32195351<ref>PMID:32195351</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6rtg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Yermw]] | ||
[[Category: Bogdanovic, X]] | [[Category: Bogdanovic, X]] | ||
[[Category: Hunte, C]] | [[Category: Hunte, C]] | ||
Current revision
Crystal structure of the UDP-bound glycosyltransferase domain from the YGT toxin
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