4MIX

PaToxG Glycosyltransferase

Summary for 4MIX

• Entry DOI: 10.2210/pdb4mix/pdb
• Descriptor: Putative insecticidal toxin, CALCIUM ION, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, ... (4 entities in total)
• Functional Keywords: tyrosine glycosylation, udp-glcnac, nucleotide-binding domain a/b/a, rossmann-like, glycosyltransferase, rho-proteins, transferase
• Biological source: Photorhabdus asymbiotica subsp. asymbiotica
• Cellular location: Secreted : C7BKP9
• Total number of polymer chains: 2
• Total formula weight: 76699.35

Authors

Bogdanovic, X.,Wirth, C.,Hunte, C. (deposition date: 2013-09-02, release date: 2013-10-16, Last modification date: 2024-11-06)

Primary citation

Jank, T.,Bogdanovic, X.,Wirth, C.,Haaf, E.,Spoerner, M.,Bohmer, K.E.,Steinemann, M.,Orth, J.H.,Kalbitzer, H.R.,Warscheid, B.,Hunte, C.,Aktories, K.
A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
Nat.Struct.Mol.Biol., 20:1273-1280, 2013

PubMed Abstract: Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans. Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain. PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc). Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells. The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known. (1)H-NMR analysis identifies PaTox as a retaining glycosyltransferase. The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.

PubMed: 24141704
DOI: 10.1038/nsmb.2688

Experimental method

X-RAY DIFFRACTION (1.8 Å)