TY - JOUR
T1 - Structural insights showing how arginine is able to be glycosylated by pathogenic effector proteins
AU - Park, Jun Bae
AU - Yoo, Youngki
AU - Cho, Hyun Soo
N1 - Publisher Copyright:
© 2018 by the The Korean Society for Biochemistry and Molecular Biology.
Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2018/12/1
Y1 - 2018/12/1
N2 - Glycosylation is one form of protein modification and plays a key role in protein stability, function, signaling regulation and even cancer. NleB and SseK are bacterial effector proteins and possess glycosyltransferase activity, even though they have different substrate preferences. NleB/SseKs transfer the GlcNAc sugar to an arginine residue of host proteins, leading to reduced NF-κB-dependent responses. By combining X-ray crystallography, NMR, molecular dynamics, enzyme kinetic assays and in vivo experiments, we demonstrated that a conserved HEN (His-Glu-Asn) motif in the active site plays a key role in enzyme catalysis and virulence. The lid-domain regulates the opening and closing of the active site and the HLH domain determines the substrate specificity. Our findings provide evidence for the enzymatic mechanism by which arginine can be glycosylated by SseK/NleB enzymes.
AB - Glycosylation is one form of protein modification and plays a key role in protein stability, function, signaling regulation and even cancer. NleB and SseK are bacterial effector proteins and possess glycosyltransferase activity, even though they have different substrate preferences. NleB/SseKs transfer the GlcNAc sugar to an arginine residue of host proteins, leading to reduced NF-κB-dependent responses. By combining X-ray crystallography, NMR, molecular dynamics, enzyme kinetic assays and in vivo experiments, we demonstrated that a conserved HEN (His-Glu-Asn) motif in the active site plays a key role in enzyme catalysis and virulence. The lid-domain regulates the opening and closing of the active site and the HLH domain determines the substrate specificity. Our findings provide evidence for the enzymatic mechanism by which arginine can be glycosylated by SseK/NleB enzymes.
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U2 - 10.5483/BMBRep.2018.51.12.269
DO - 10.5483/BMBRep.2018.51.12.269
M3 - Article
C2 - 30463645
AN - SCOPUS:85059225811
VL - 51
SP - 609
EP - 610
JO - BMB Reports
JF - BMB Reports
SN - 1976-6696
IS - 12
ER -