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O-GlcNAc transferase

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== Structural highlights ==
== Structural highlights ==
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<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.
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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.
</StructureSection>
</StructureSection>

Revision as of 12:57, 24 July 2019

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

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3D structures of O-GlcNAc transferase

Updated on 24-July-2019


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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Michal Harel, Alexander Berchansky

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