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Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase-2
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The family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (ppGalNAcTs) is unique among glycosyltransferases, containing both catalytic and lectin domains that we have previously shown to be closely associated. Here we describe the x-ray crystal structures of human ppGalNAcT-2 (hT2) bound to the product UDP at 2.75 A resolution and to UDP and an acceptor peptide substrate EA2 (PTTDSTTPAPTTK) at 1.64 A resolution. The conformations of both UDP and residues Arg362-Ser372 vary greatly between the two structures. In the hT2-UDP-EA2 complex, residues Arg362-Ser373 comprise a loop that forms a lid over UDP, sealing it in the active site, whereas in the hT2-UDP complex this loop is folded back, exposing UDP to bulk solvent. EA2 binds in a shallow groove with threonine 7 positioned consistent with in vitro data showing it to be the preferred site of glycosylation. The relative orientations of the hT2 catalytic and lectin domains differ dramatically from that of murine ppGalNAcT-1 and also vary considerably between the two hT2 complexes. Indeed, in the hT2-UDP-EA2 complex essentially no contact is made between the catalytic and lectin domains except for the peptide bridge between them. Thus, the hT2 structures reveal an unexpected flexibility between the catalytic and lectin domains and suggest a new mechanism used by hT2 to capture glycosylated substrates. Kinetic analysis of hT2 lacking the lectin domain confirmed the importance of this domain in acting on glycopeptide but not peptide substrates. The structure of the hT2-UDP-EA2 complex also resolves long standing questions regarding ppGalNAcT acceptor substrate specificity.
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“As an example, glycosylation of the synthetic peptide EA2 (PTTDSTTPAPTTK)—derived from Rattus norvegicus submandibular apomucin 10 (MUC10)—has been demonstrated in various in vitro assays in the presence of soluble GalNAc-T2 [6, 14, 15].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [15]
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“In contrast, O-glycosylation of eukaryotic target sites using a truncated form of the human glycosyltransferase GalNAc-T2 has been shown without altering the target peptide sequence [6, 9, 14, 15].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [15]
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“Previous in vitro studies with GalNAc-T2 have identified Thr7 in the synthetic EA2 peptide sequence [14, 15] and Thr9 in the MUC5AC peptide as preferred glycosylation sites [31].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [15]
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Metadata
- Authors
- Fritz, T. A., Raman, J., & Tabak, L. A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Tabak, Lawrence A.
- ORCID
- Tabak, Lawrence A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-03
- Volume
- 281
- Issue
- 13
- Pages
- 8613-8619
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1992607565
- Cited by
- 163
- References
- 48
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 14 · 2023: 3 · 2022: 4 · 2021: 5 · 2020: 10 · 2019: 10 · 2018: 8 · 2017: 6 · 2016: 10 · 2015: 5 · 2014: 11 · 2013: 6 · 2012: 6
- FWCI
- 4.32
- Type
- journal article
- Language
- en
- Update notices
- erratum (2006-08-25)
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- catalytic domain, lectin domain, domain flexibility, substrate recognition, acceptor substrate specificity, glycosylation sites
- MeSH terms
- Polypeptide N-acetylgalactosaminyltransferase, Amino Acid Sequence, Binding Sites, Glycosylation, Humans, Hydrogen Bonding, Isoenzymes, Kinetics, Manganese, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Threonine, Uridine Diphosphate N-Acetylgalactosamine, Conserved Sequence, N-Acetylgalactosaminyltransferases, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Crystallography, X-Ray, HL-60 Cells, Catalytic Domain, Lectins, Intracellular Signaling Peptides and Proteins, Hydrophobic and Hydrophilic Interactions
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