O-GlcNAc transferase
From Proteopedia
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| - | '''O-GlcNac transferase''' (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see [[Human O-GlcNAc transferase]]. | + | '''O-GlcNac transferase''' (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation<ref>PMID:26237509</ref>. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. '''MurG:UDP-GlcNac''' is an OGT which forms glycosidic linkage between N-acetyl muramyl pentapeptide and N-acetyl glycosamine in the synthesis of bacterial cell wall<ref>PMID:12538870</ref>. |
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| + | For details see [[Human O-GlcNAc transferase]]. | ||
==3D structures of O-GlcNAc transferase== | ==3D structures of O-GlcNAc transferase== | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 06:48, 8 June 2016
O-GlcNac transferase (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation[1]. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. MurG:UDP-GlcNac is an OGT which forms glycosidic linkage between N-acetyl muramyl pentapeptide and N-acetyl glycosamine in the synthesis of bacterial cell wall[2].
For details see Human O-GlcNAc transferase.
3D structures of O-GlcNAc transferase
Updated on 08-June-2016
References
- ↑ Pathak S, Alonso J, Schimpl M, Rafie K, Blair DE, Borodkin VS, Schuttelkopf AW, Albarbarawi O, van Aalten DM. The active site of O-GlcNAc transferase imposes constraints on substrate sequence. Nat Struct Mol Biol. 2015 Aug 3. doi: 10.1038/nsmb.3063. PMID:26237509 doi:http://dx.doi.org/10.1038/nsmb.3063
- ↑ Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):845-9. Epub 2003 Jan 21. PMID:12538870 doi:10.1073/pnas.0235749100
