O-GlcNAc transferase

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**[[3s2u]] - MurG + UDP-GlcNac – ''Pseudomonas aeruginosa''<br />
**[[3s2u]] - MurG + UDP-GlcNac – ''Pseudomonas aeruginosa''<br />
-
**[[1nlm]] – EcMurG + UDP-acetylglucosamine – ''Escherichia coli''<br />
+
**[[1nlm]] – EcMurG + UDP-GlcNac – ''Escherichia coli''<br />
**[[1f0k]] – EcMurG <br />
**[[1f0k]] – EcMurG <br />

Revision as of 06:53, 8 June 2016

Template:STRUCTURE 1nlm


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

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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