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O-GlcNAc transferase

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{{STRUCTURE_1nlm| PDB=1nlm | SIZE=350| SCENE= |right|CAPTION=E. coli O-GlcNAc transferase dimer complex with UDP-GlcNAc and glycerol, [[1nlm]] }}
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<StructureSection load='4gz5' size='350' side='right' caption='O-GlcNAc transferase complex with UDP-GlcNAc and sulfate (PDB entry [[4gz5]])' scene='46/468106/Cv/1'>
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== Function ==
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'''O-GlcNac transferase''' or '''O-glycosyltransferase''' (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]].
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'''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 ==
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For details see [[Human O-GlcNAc transferase]].
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<scene name='46/468106/Cv/5'>OGT active site residues involved in the addition reaction</scene><ref>PMID:23103939</ref>. Water molecule is shown as red sphere.
==3D structures of O-GlcNAc transferase==
==3D structures of O-GlcNAc transferase==
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[[O-GlcNAc transferase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*O-GlcNAc transferase
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**[[1fo8]], [[1fo9]], [[1foa]] - rOGT catalytic domain – rabbit
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**[[1w3b]] – hOGT TPR domain – human
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**[[2gak]] – mOGT – mouse
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**[[2j0a]], [[3otk]] – mOGT catalytic domain (mutant)<br />
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**[[5a01]] - DmOGT TPR and catalytic domains – ''Drosophila melanogaster''<br />
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**[[5djs]] - OGT TPR and catalytic domains (mutant) – ''Thermobaculum terrenum''<br />
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*O-GlcNAc transferase binary complexes
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**[[2am3]], [[2am4]] - rOGT catalytic domain + UDP-glucose derivative
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**[[2am5]] - rOGT catalytic domain + UDP
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**[[2j0b]] - mOGT catalytic domain (mutant) + UDP
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**[[2apc]] - rOGT catalytic domain + UDP-GlcNAc phosphonate
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**[[2gam]] - mOGT + b-D-galactose + N-acetyl-galactosamine
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**[[3pe3]], [[3pe4]] – hOGT TPR and catalytic domains+ peptide substrate
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**[[2jlb]] – XcOGT + UDP-GlcNAc phosphonate analog – ''Xanthomonas campestris''
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**[[2xgm]] – XcOGT + alloxan + mesoxalylurea
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**[[2xgo]] - XcOGT + UDP-GlcNAc
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**[[2xgs]] - XcOGT + UDP
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**[[1nlm]] – OGT + UDP-acetylglucosamine – ''Escherichia coli''<br />
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**[[4cdr]] - hOGT TPR and catalytic domains + UDP-peptide conjugate<br />
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**[[5bnw]], [[3tax]] - hOGT TPR and catalytic domains + substrate peptide <br />
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**[[4gz5]], [[4gz6]] - hOGT TPR and catalytic domains + UDP-GlcNAc<br />
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*OGT higher complexes
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**[[2xgm]] – XcOGT + alloxan + mesoxalylurea<br />
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**[[3ee5]] – hOGT + UDP + NAG + galactose + naphthalene derivative<br />
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**[[4ay5]], [[4gyw]], [[4gyy]], [[4gz3]] - hOGT TPR and catalytic domains + UDP + NAG + glycopeptide<br />
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**[[4n39]], [[4n3a]], [[4n3b]], [[4n3c]] - hOGT TPR and catalytic domains + UDP + host cell factor peptide<br />
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**[[4xi9]], [[4xif]], [[5c1d]], [[4ay6]] - hOGT TPR and catalytic domains + UDP-GlcNac + substrate peptide<br />
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**[[4pqg]] - OGT TPR and catalytic domains + UDP + GlcNac – Streptococcus pneumoniae<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

O-GlcNAc transferase complex with UDP-GlcNAc and sulfate (PDB entry 4gz5)

Drag the structure with the mouse to rotate

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
  3. ↑ 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

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