Cited by 175Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisEnzyme Structure and Function

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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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Fritz, Timothy A., Raman, Jayalakshmi, Tabak, Lawrence A.·2006·Journal of Biological Chemistry

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Abstract

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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Additional file 2 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26122880
Additional file 5 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740310
Additional file 12 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740331
Additional file 3 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740304
Additional file 4 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740307
Additional file 10 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740325
Additional file 15 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740340
Additional file 7 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740316
Additional file 14 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740337
Additional file 11 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740328
Additional file 6 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740313
Additional file 13 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740334
Additional file 1 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26122645
Additional file 8 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740319
Additional file 9 of Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks
Coninck, T. D., Gippert, G. P., Henrissat, B., Desmet, T., & Damme, E. J. M. V. (2024) · Figshare · doi:10.6084/m9.figshare.26740322
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BindingDB (2021) · UC San Diego · doi:10.7270/q2988bdq
BindingDB Entry 50032103: An efficient approach to the discovery of potent inhibitors against glycosyltransferases.
BindingDB (2011) · UC San Diego · doi:10.7270/q2ws8tfd

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)
DOI: 10.1074/jbc.m513590200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5329 d)
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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Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase-2

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