5H62

Structure of Transferase mutant-C23S,C199S

Summary for 5H62

• Entry DOI: 10.2210/pdb5h62/pdb
• Related: 5H5Y 5H60 5H61 5H63
• Descriptor: Transferase, 1,2-ETHANEDIOL, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 80393.20

Authors

Park, J.B.,Yoo, Y.,Kim, J. (deposition date: 2016-11-10, release date: 2017-12-27, Last modification date: 2024-03-20)

Primary citation

Park, J.B.,Kim, Y.H.,Yoo, Y.,Kim, J.,Jun, S.H.,Cho, J.W.,El Qaidi, S.,Walpole, S.,Monaco, S.,Garcia-Garcia, A.A.,Wu, M.,Hays, M.P.,Hurtado-Guerrero, R.,Angulo, J.,Hardwidge, P.R.,Shin, J.S.,Cho, H.S.
Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
Nat Commun, 9:4283-4283, 2018

PubMed Abstract: The bacterial effector proteins SseK and NleB glycosylate host proteins on arginine residues, leading to reduced NF-κB-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 Si mechanism, explain differences in activities among these effectors, and have implications for future drug development against enteric pathogens.

PubMed: 30327479
DOI: 10.1038/s41467-018-06680-6

Experimental method

X-RAY DIFFRACTION (1.66 Å)