Structural highlights
37on is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 3.08Å |
| Ligands: | BMA, EDO, GOL, MAN, MN, NAG, PG4, UDP |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
GALT5_DROME Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:12829714, PubMed:18669915). It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers EA2 as substrate (PubMed:12829714). In the larval midgut, required for O-glycosylation of apical and luminal proteins within copper cells enabling proper gut acidification (PubMed:22157008).[1] [2] [3]
References
- ↑ Ten Hagen KG, Tran DT, Gerken TA, Stein DS, Zhang Z. Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster. J Biol Chem. 2003 Sep 12;278(37):35039-48. doi: 10.1074/jbc.M303836200. Epub 2003 , Jun 26. PMID:12829714 doi:https://dx.doi.org/10.1074/jbc.M303836200
- ↑ Gerken TA, Ten Hagen KG, Jamison O. Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs. Glycobiology. 2008 Nov;18(11):861-70. doi: 10.1093/glycob/cwn073. Epub 2008 Jul , 31. PMID:18669915 doi:https://dx.doi.org/10.1093/glycob/cwn073
- ↑ Tran DT, Zhang L, Zhang Y, Tian E, Earl LA, Ten Hagen KG. Multiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila. J Biol Chem. 2012 Feb 17;287(8):5243-52. doi: 10.1074/jbc.M111.306159. Epub 2011 , Dec 7. PMID:22157008 doi:https://dx.doi.org/10.1074/jbc.M111.306159