O-GlcNAc transferase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:18, 17 July 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='4gz5' size='350' side='right' caption='O-GlcNAc transferase complex with UDP-GlcNAc (stick model) and sulfate (PDB entry [[4gz5]])' scene=''>
+
<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'>
== 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''' 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>.
For details see [[Human O-GlcNAc transferase]].
For details see [[Human O-GlcNAc transferase]].
Line 7: Line 8:
== Structural highlights ==
== Structural highlights ==
-
OGT active site residues involved in the addition reaction<ref>PMID:23103939</ref>.
+
<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.
-
</StructureSection>
+
==3D structures of O-GlcNAc transferase==
==3D structures of O-GlcNAc transferase==
 +
[[O-GlcNAc transferase 3D structures]]
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
</StructureSection>
-
{{#tree:id=OrganizedByTopic|openlevels=0|
+
-
 
+
-
*O-GlcNAc transferase
+
-
 
+
-
**[[1fo8]], [[1fo9]], [[1foa]] - rOGT catalytic domain – rabbit
+
-
 
+
-
**[[1w3b]] – hOGT TPR domain – human
+
-
 
+
-
**[[2gak]] – mOGT – mouse
+
-
 
+
-
**[[2j0a]], [[3otk]] – mOGT catalytic domain (mutant)<br />
+
-
**[[5a01]] - DmOGT TPR and catalytic domains – ''Drosophila melanogaster''<br />
+
-
**[[5djs]] - OGT TPR and catalytic domains (mutant) – ''Thermobaculum terrenum''<br />
+
-
 
+
-
 
+
-
*O-GlcNAc transferase binary complexes
+
-
 
+
-
**[[2am3]], [[2am4]] - rOGT catalytic domain + UDP-glucose derivative
+
-
 
+
-
**[[2am5]] - rOGT catalytic domain + UDP
+
-
 
+
-
**[[2j0b]] - mOGT catalytic domain (mutant) + UDP
+
-
 
+
-
**[[2apc]] - rOGT catalytic domain + UDP-GlcNAc phosphonate
+
-
 
+
-
**[[3pe3]], [[3pe4]] – hOGT TPR and catalytic domains+ peptide substrate
+
-
 
+
-
**[[2jlb]] – XcOGT + UDP-GlcNAc phosphonate analog – ''Xanthomonas campestris''
+
-
 
+
-
**[[2xgm]] – XcOGT + alloxan + mesoxalylurea
+
-
 
+
-
**[[2xgo]] - XcOGT + UDP-GlcNAc
+
-
 
+
-
**[[2xgs]] - XcOGT + UDP
+
-
 
+
-
**[[4cdr]] - hOGT TPR and catalytic domains + UDP-peptide conjugate<br />
+
-
**[[5bnw]], [[3tax]] - hOGT TPR and catalytic domains + substrate peptide <br />
+
-
**[[4gz5]], [[4gz6]] - hOGT TPR and catalytic domains + UDP-GlcNAc<br />
+
-
 
+
-
*OGT higher complexes
+
-
 
+
-
**[[2xgm]] – XcOGT + alloxan + mesoxalylurea<br />
+
-
**[[3ee5]] – hOGT + UDP + NAG + galactose + naphthalene derivative<br />
+
-
**[[4ay5]], [[4gyw]], [[4gyy]], [[4gz3]] - hOGT TPR and catalytic domains + UDP + NAG + glycopeptide<br />
+
-
**[[4n39]], [[4n3a]], [[4n3b]], [[4n3c]] - hOGT TPR and catalytic domains + UDP + host cell factor 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 />
+
-
**[[2gam]] - mOGT + b-D-galactose + N-acetyl-galactosamine<br />
+
-
 
+
-
*MurG:UDP-GlcNac
+
-
 
+
-
**[[3s2u]] - MurG + UDP-GlcNac – ''Pseudomonas aeruginosa''<br />
+
-
**[[1nlm]] – EcMurG + UDP-GlcNac – ''Escherichia coli''<br />
+
-
**[[1f0k]] – EcMurG <br />
+
-
}}
 
== 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/O-GlcNAc_transferase"
Personal tools