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O-GlcNAc transferase
From Proteopedia
(Difference between revisions)
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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. | <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. | ||
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| + | ==3D structures of O-GlcNAc transferase== | ||
| + | [[O-GlcNAc transferase 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *O-GlcNAc transferase | + | *O-GlcNAc transferase Domains: TPR 16-400; TPR+catalytic 323-1041; P110 197-915 |
| - | + | ||
| - | + | ||
**[[1w3b]] – hOGT TPR domain – human | **[[1w3b]] – hOGT TPR domain – human | ||
| + | |||
| + | **[[6eou]] - hOGT TPR domain (mutant) <br /> | ||
| + | **[[1fo8]], [[1fo9]], [[1foa]] - rOGT catalytic domain – rabbit | ||
**[[2gak]] – mOGT – mouse | **[[2gak]] – mOGT – mouse | ||
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*O-GlcNAc transferase binary complexes | *O-GlcNAc transferase binary complexes | ||
| + | **[[3pe3]], [[3pe4]] – hOGT TPR and catalytic domains+ peptide substrate | ||
| + | |||
| + | **[[4cdr]] - hOGT TPR and catalytic domains + UDP-peptide conjugate<br /> | ||
| + | **[[5bnw]], [[3tax]], [[6ibo]] - hOGT TPR and catalytic domains + substrate peptide <br /> | ||
| + | **[[4gz5]], [[4gz6]] - hOGT TPR and catalytic domains + UDP-GlcNAc<br /> | ||
| + | **[[6e37]], [[5vif]], [[5vie]] - hOGT P110 subunit + peptide<br /> | ||
| + | **[[5hgv]] - hOGT P110 subunit (mutant) + peptide<br /> | ||
| + | **[[5nps]], [[5npr]] - hOGT P110 subunit + inhibitor<br /> | ||
**[[2am3]], [[2am4]] - rOGT catalytic domain + UDP-glucose derivative | **[[2am3]], [[2am4]] - rOGT catalytic domain + UDP-glucose derivative | ||
**[[2am5]] - rOGT catalytic domain + UDP | **[[2am5]] - rOGT catalytic domain + UDP | ||
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| - | **[[2j0b]] - mOGT catalytic domain (mutant) + UDP | ||
**[[2apc]] - rOGT catalytic domain + UDP-GlcNAc phosphonate | **[[2apc]] - rOGT catalytic domain + UDP-GlcNAc phosphonate | ||
| - | **[[ | + | **[[2j0b]] - mOGT catalytic domain (mutant) + UDP |
**[[2jlb]] – XcOGT + UDP-GlcNAc phosphonate analog – ''Xanthomonas campestris'' | **[[2jlb]] – XcOGT + UDP-GlcNAc phosphonate analog – ''Xanthomonas campestris'' | ||
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**[[2xgs]] - XcOGT + UDP | **[[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 | *OGT higher complexes | ||
| - | **[[2xgm]] – XcOGT + alloxan + mesoxalylurea<br /> | ||
**[[3ee5]] – hOGT + UDP + NAG + galactose + naphthalene derivative<br /> | **[[3ee5]] – hOGT + UDP + NAG + galactose + naphthalene derivative<br /> | ||
**[[4ay5]], [[4gyw]], [[4gyy]], [[4gz3]] - hOGT TPR and catalytic domains + UDP + NAG + glycopeptide<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 /> | **[[4n39]], [[4n3a]], [[4n3b]], [[4n3c]] - hOGT TPR and catalytic domains + UDP + host cell factor peptide<br /> | ||
| - | **[[4xi9]], [[4xif | + | **[[4xi9]], [[4xif]], [[4ay6]] - hOGT TPR and catalytic domains + UDP-GlcNac + substrate peptide<br /> |
| - | **[[ | + | **[[6ma5]], [[6ma4]], [[6ma3]], [[6ma2]], [[6ma1]] - hOGT P110 subunit + host cell factor peptide + inhibitor<br /> |
| + | **[[5lvv]] - hOGT P110 subunit + UDP + NAG<br /> | ||
| + | **[[5c1d]], [[5bnw]] - hOGT P110 subunit + UDP-GlcNac + peptide<br /> | ||
**[[2gam]] - mOGT + b-D-galactose + N-acetyl-galactosamine<br /> | **[[2gam]] - mOGT + b-D-galactose + N-acetyl-galactosamine<br /> | ||
| + | **[[2xgm]] – XcOGT + alloxan + mesoxalylurea<br /> | ||
| + | **[[4pqg]] - OGT TPR and catalytic domains + UDP + GlcNac – ''Streptococcus pneumoniae''<br /> | ||
*MurG:UDP-GlcNac | *MurG:UDP-GlcNac | ||
Revision as of 09:46, 12 November 2019
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3D structures of O-GlcNAc transferase
Updated on 12-November-2019
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
