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1. (CSDB ID: 7330) | report error |
| a-D-Galp-(1-3)-a-D-Glcp-(1-3)-a-L-Fucp-(1-2)-b-D-Galp-(1-3)-a-D-GlcpNAc-(1--/(->4)Pro154-Skp1(peptide)/ | Show graphically |
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Toxoplasma gondii RH
(NCBI TaxID 383379,
species name lookup)
, ICD11: XN896 ]
uga.eduSkp1, a subunit of E3 Skp1/Cullin-1/F-box protein ubiquitin ligases, is modified by a prolyl hydroxylase that mediates O2 regulation of the social amoeba Dictyostelium and the parasite Toxoplasma gondii The full effect of hydroxylation requires modification of the hydroxyproline by a pentasaccharide that, in Dictyostelium, influences Skp1 structure to favor assembly of Skp1/F-box protein subcomplexes. In Toxoplasma, the presence of a contrasting penultimate sugar assembled by a different glycosyltransferase enables testing of the conformational control model. To define the final sugar and its linkage, here we identified the glycosyltransferase that completes the glycan and found that it is closely related to glycogenin, an enzyme that may prime glycogen synthesis in yeast and animals. However, the Toxoplasma enzyme catalyzes formation of a Galα1,3Glcα linkage rather than the Glcα1,4Glcα linkage formed by glycogenin. Kinetic and crystallographic experiments showed that the glycosyltransferase Gat1 is specific for Skp1 in Toxoplasma and also in another protist, the crop pathogen Pythium ultimum The fifth sugar is important for glycan function as indicated by the slow-growth phenotype of gat1Δ parasites. Computational analyses indicated that, despite the sequence difference, the Toxoplasma glycan still assumes an ordered conformation that controls Skp1 structure and revealed the importance of nonpolar packing interactions of the fifth sugar. The substitution of glycosyltransferases in Toxoplasma and Pythium by an unrelated bifunctional enzyme that assembles a distinct but structurally compatible glycan in Dictyostelium is a remarkable case of convergent evolution, which emphasizes the importance of the terminal α-galactose and establishes the phylogenetic breadth of Skp1 glycoregulation.
NMR, molecular dynamics, glycosyltransferase, Post-translational modification, nuclear magnetic resonance (NMR), molecular dynamics simulation, Toxoplasma, Toxoplasma gondii, post-translational modification (PTM), cytoplasmic glycosylation, E3 ubiquitin ligase, glycogenin, Pythium, s: X-ray crystallography, SCF, Skp1
Structure type: oligomer|
2. (CSDB ID: 8159) | report error |
| a-D-Glcp-(1-3)-a-L-Fucp-(1-2)-b-D-Galp-(1-3)-a-D-GlcpNAc-(1--/(->4)Pro154-Skp1(peptide)/ | Show graphically |
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Toxoplasma gondii RH
(NCBI TaxID 383379,
species name lookup)
, ICD11: XN896 ]uga.eduSkp1, a subunit of E3 Skp1/Cullin-1/F-box protein ubiquitin ligases, is modified by a prolyl hydroxylase that mediates O2 regulation of the social amoeba Dictyostelium and the parasite Toxoplasma gondii The full effect of hydroxylation requires modification of the hydroxyproline by a pentasaccharide that, in Dictyostelium, influences Skp1 structure to favor assembly of Skp1/F-box protein subcomplexes. In Toxoplasma, the presence of a contrasting penultimate sugar assembled by a different glycosyltransferase enables testing of the conformational control model. To define the final sugar and its linkage, here we identified the glycosyltransferase that completes the glycan and found that it is closely related to glycogenin, an enzyme that may prime glycogen synthesis in yeast and animals. However, the Toxoplasma enzyme catalyzes formation of a Galα1,3Glcα linkage rather than the Glcα1,4Glcα linkage formed by glycogenin. Kinetic and crystallographic experiments showed that the glycosyltransferase Gat1 is specific for Skp1 in Toxoplasma and also in another protist, the crop pathogen Pythium ultimum The fifth sugar is important for glycan function as indicated by the slow-growth phenotype of gat1Δ parasites. Computational analyses indicated that, despite the sequence difference, the Toxoplasma glycan still assumes an ordered conformation that controls Skp1 structure and revealed the importance of nonpolar packing interactions of the fifth sugar. The substitution of glycosyltransferases in Toxoplasma and Pythium by an unrelated bifunctional enzyme that assembles a distinct but structurally compatible glycan in Dictyostelium is a remarkable case of convergent evolution, which emphasizes the importance of the terminal α-galactose and establishes the phylogenetic breadth of Skp1 glycoregulation.
NMR, molecular dynamics, glycosyltransferase, Post-translational modification, nuclear magnetic resonance (NMR), molecular dynamics simulation, Toxoplasma, Toxoplasma gondii, post-translational modification (PTM), cytoplasmic glycosylation, E3 ubiquitin ligase, glycogenin, Pythium, s: X-ray crystallography, SCF, Skp1
Structure type: oligomer|
3. (CSDB ID: 8160) | report error |
| a-D-Galp-(1-3)-a-D-Galp-(1-3)-a-L-Fucp-(1-2)-b-D-Galp-(1-3)-a-D-GlcpNAc-(1--/(->4)Pro143-Skp1(peptide)/ | Show graphically |
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Dictyostelium discoideum
(NCBI TaxID 44689,
species name lookup)
uga.eduSkp1, a subunit of E3 Skp1/Cullin-1/F-box protein ubiquitin ligases, is modified by a prolyl hydroxylase that mediates O2 regulation of the social amoeba Dictyostelium and the parasite Toxoplasma gondii The full effect of hydroxylation requires modification of the hydroxyproline by a pentasaccharide that, in Dictyostelium, influences Skp1 structure to favor assembly of Skp1/F-box protein subcomplexes. In Toxoplasma, the presence of a contrasting penultimate sugar assembled by a different glycosyltransferase enables testing of the conformational control model. To define the final sugar and its linkage, here we identified the glycosyltransferase that completes the glycan and found that it is closely related to glycogenin, an enzyme that may prime glycogen synthesis in yeast and animals. However, the Toxoplasma enzyme catalyzes formation of a Galα1,3Glcα linkage rather than the Glcα1,4Glcα linkage formed by glycogenin. Kinetic and crystallographic experiments showed that the glycosyltransferase Gat1 is specific for Skp1 in Toxoplasma and also in another protist, the crop pathogen Pythium ultimum The fifth sugar is important for glycan function as indicated by the slow-growth phenotype of gat1Δ parasites. Computational analyses indicated that, despite the sequence difference, the Toxoplasma glycan still assumes an ordered conformation that controls Skp1 structure and revealed the importance of nonpolar packing interactions of the fifth sugar. The substitution of glycosyltransferases in Toxoplasma and Pythium by an unrelated bifunctional enzyme that assembles a distinct but structurally compatible glycan in Dictyostelium is a remarkable case of convergent evolution, which emphasizes the importance of the terminal α-galactose and establishes the phylogenetic breadth of Skp1 glycoregulation.
NMR, molecular dynamics, glycosyltransferase, Post-translational modification, nuclear magnetic resonance (NMR), molecular dynamics simulation, Toxoplasma, Toxoplasma gondii, post-translational modification (PTM), cytoplasmic glycosylation, E3 ubiquitin ligase, glycogenin, Pythium, s: X-ray crystallography, SCF, Skp1
Structure type: oligomer|
4. (CSDB ID: 23666) | report error |
| Thr-(2-6)-b-D-ManpNAcA-(1-4)-b-D-GlcpNAc3NAcA-(1-3)-b-D-GlcpNAc | Show graphically |
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Methanococcus voltae
(NCBI TaxID 2188,
species name lookup)
queensu.caRecent advances in the field of prokaryotic N-glycosylation have established a foundation for the pathways and proteins involved in this important post-translational protein modification process. To continue the study of the Methanococcus voltae N-glycosylation pathway, characteristics of known eukaryotic, bacterial and archaeal proteins involved in the N-glycosylation process were examined and used to select candidate M. voltae genes for investigation as potential glycosyl transferase and flippase components. Targeted genes were knocked-out via linear gene replacement and the resulting effects on N-glycan assembly were identified through flagellin and surface (S)-layer protein glycosylation defects. This study reports the finding that deletion of two putative M. voltae glycosyl transferases, designated aglC (archaeal glycosylation) and aglK, interfered with proper N-glycosylation. This resulted in flagellin and S-layer proteins with significantly reduced apparent molecular masses, loss of flagella assembly and absence of glycan attachment. Given previous knowledge of both the N-glycosylation pathway in M. voltae and general characteristics of N-glycosylation components, it appears that AglC and AglK are involved in the biosynthesis or transfer of diacetylated glucuronic acid within the glycan structure. In addition, a knockout of the putative flippase candidate gene (Mv891) had no effect on N-glycosylation but did result in the production of giant cells with diameters three to four times that of wild type cells
biosynthesis, transfer, structure, gene, Bacterial, microbiology, potential, cell, molecular, Research, acid, transferase, type, immunology, protein, wild type, Genes, glycan, biological, assembly, putative, production, reduced, modification, surface, glucuronic acid, molecular mass, component, time, linear, glycosyl, glycosylation, loss, pathway, cells, proteins, effect, S-layer, transferases, S layer, glycosyl transferases, characteristics, attachment, absence, flagella, Flagellin, archaeal protein, Archaeal Proteins, Methanococcus
Structure type: oligomer| New query | Export IDs | Home | Help |
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