O-GlcNAc transferase

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**[[2apc]] - rOGT catalytic domain + UDP-GlcNAc phosphonate
**[[2apc]] - rOGT catalytic domain + UDP-GlcNAc phosphonate
- 
-
**[[2gam]] - mOGT + b-D-galactose + N-acetyl-galactosamine
 
**[[3pe3]], [[3pe4]] – hOGT TPR and catalytic domains+ peptide substrate
**[[3pe3]], [[3pe4]] – hOGT TPR and catalytic domains+ peptide substrate
Line 58: Line 56:
**[[4xi9]], [[4xif]], [[5c1d]], [[4ay6]] - hOGT TPR and catalytic domains + UDP-GlcNac + substrate peptide<br />
**[[4xi9]], [[4xif]], [[5c1d]], [[4ay6]] - hOGT TPR and catalytic domains + UDP-GlcNac + substrate peptide<br />
**[[4pqg]] - OGT TPR and catalytic domains + UDP + GlcNac – Streptococcus pneumoniae<br />
**[[4pqg]] - OGT TPR and catalytic domains + UDP + GlcNac – Streptococcus pneumoniae<br />
 +
**[[2gam]] - mOGT + b-D-galactose + N-acetyl-galactosamine<br />
*MurG:UDP-GlcNac
*MurG:UDP-GlcNac

Revision as of 06:57, 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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