5h60

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'''Unreleased structure'''
 
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The entry 5h60 is ON HOLD
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==Structure of Transferase mutant-C23S,C199S==
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<StructureSection load='5h60' size='340' side='right'caption='[[5h60]], [[Resolution|resolution]] 3.64&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5h60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H60 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.64&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h60 OCA], [https://pdbe.org/5h60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h60 RCSB], [https://www.ebi.ac.uk/pdbsum/5h60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h60 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SSEK1_SALTY SSEK1_SALTY] Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:23955153, PubMed:28069818, PubMed:28522607). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins TRADD and, to a lower extent, FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:23955153, PubMed:28069818). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2, leading to inhibit NF-kappa-B signaling (PubMed:28522607). Catalyzes GlcNAcylation of host tubulin-folding cofactor TBCB, thereby promoting microtubule stability (PubMed:32366039). Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32366039).<ref>PMID:23955153</ref> <ref>PMID:28069818</ref> <ref>PMID:28522607</ref> <ref>PMID:32366039</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bacterial effector proteins SseK and NleB glycosylate host proteins on arginine residues, leading to reduced NF-kappaB-dependent responses to infection. Salmonella SseK1 and SseK2 are E. coli NleB1 orthologs that behave as NleB1-like GTs, although they differ in protein substrate specificity. Here we report that these enzymes are retaining glycosyltransferases composed of a helix-loop-helix (HLH) domain, a lid domain, and a catalytic domain. A conserved HEN motif (His-Glu-Asn) in the active site is important for enzyme catalysis and bacterial virulence. We observe differences between SseK1 and SseK2 in interactions with substrates and identify substrate residues that are critical for enzyme recognition. Long Molecular Dynamics simulations suggest that the HLH domain determines substrate specificity and the lid-domain regulates the opening of the active site. Overall, our data suggest a front-face SNi mechanism, explain differences in activities among these effectors, and have implications for future drug development against enteric pathogens.
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Authors: Park, J.B., Yoo, Y., Kim, J.
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Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.,Park JB, Kim YH, Yoo Y, Kim J, Jun SH, Cho JW, El Qaidi S, Walpole S, Monaco S, Garcia-Garcia AA, Wu M, Hays MP, Hurtado-Guerrero R, Angulo J, Hardwidge PR, Shin JS, Cho HS Nat Commun. 2018 Oct 16;9(1):4283. doi: 10.1038/s41467-018-06680-6. PMID:30327479<ref>PMID:30327479</ref>
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Description: Structure of Transferase mutant-C23S,C199S
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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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[[Category: Yoo, Y]]
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<div class="pdbe-citations 5h60" style="background-color:#fffaf0;"></div>
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[[Category: Kim, J]]
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== References ==
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[[Category: Park, J.B]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Kim J]]
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[[Category: Park JB]]
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[[Category: Yoo Y]]

Current revision

Structure of Transferase mutant-C23S,C199S

PDB ID 5h60

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