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| Title | Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 14, Page 5785-5785, Year 2023 |
| Publish date | May 10, 2023 (structure data deposition date) |
Authors | Piniello, B. / Macias-Leon, J. / Miyazaki, S. / Garcia-Garcia, A. / Companon, I. / Ghirardello, M. / Taleb, V. / Veloz, B. / Corzana, F. / Miyagawa, A. ...Piniello, B. / Macias-Leon, J. / Miyazaki, S. / Garcia-Garcia, A. / Companon, I. / Ghirardello, M. / Taleb, V. / Veloz, B. / Corzana, F. / Miyagawa, A. / Rovira, C. / Hurtado-Guerrero, R. |
External links | Nat Commun / PubMed:37723184 |
| Methods | X-ray diffraction |
| Resolution | 1.76 - 2.8 Å |
| Structure data | ![]() PDB-8p0o: ![]() PDB-8p0p: ![]() PDB-8p0q: |
| Chemicals | ![]() ChemComp-EDO: ![]() ChemComp-GDU: ![]() ChemComp-HOH: ![]() ChemComp-U2F: ![]() ChemComp-UDP: |
| Source |
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Keywords | TRANSFERASE / N-glycosylation / Asn tautomeric form / AAD / Glycosyltransferase / GT-B |
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aggregatibacter aphrophilus (bacteria)
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