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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SSEK2_SALTY SSEK2_SALTY] Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions (PubMed:28522607). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab1 GTPase, thereby preventing GTPase activity and leading to impaired host vesicular protein transport (By similarity). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells (PubMed:28522607).[UniProtKB:P0DUJ8]<ref>PMID:28522607</ref>  
[https://www.uniprot.org/uniprot/SSEK2_SALTY SSEK2_SALTY] Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions (PubMed:28522607). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab1 GTPase, thereby preventing GTPase activity and leading to impaired host vesicular protein transport (By similarity). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells (PubMed:28522607).[UniProtKB:P0DUJ8]<ref>PMID:28522607</ref>  
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== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Latest revision as of 09:15, 20 March 2024

Structure of Transferase mutant-C23S,C199S

5h63, resolution 1.92Å

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