O-GlcNAc transferase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='4gz5' size=' | + | <StructureSection load='4gz5' size='450' side='right' caption='O-GlcNAc transferase complex with UDP-GlcNAc and sulfate (PDB entry [[4gz5]])' scene='46/468106/Cv/1'> |
== Function == | == Function == | ||
'''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>. | '''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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== Structural highlights == | == Structural highlights == | ||
| - | OGT active site residues involved in the addition reaction<ref>PMID:23103939</ref>. | + | <scene name='46/468106/Cv/4'>OGT active site residues involved in the addition reaction</scene><ref>PMID:23103939</ref>. Water molecule is shown as red sphere. |
</StructureSection> | </StructureSection> | ||
Revision as of 12:23, 8 June 2016
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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
- ↑ Lazarus MB, Jiang J, Gloster TM, Zandberg WF, Whitworth GE, Vocadlo DJ, Walker S. Structural snapshots of the reaction coordinate for O-GlcNAc transferase. Nat Chem Biol. 2012 Dec;8(12):966-8. doi: 10.1038/nchembio.1109. Epub 2012 Oct, 28. PMID:23103939 doi:http://dx.doi.org/10.1038/nchembio.1109
