6EOU

O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F

Summary for 6EOU

Entry DOI	10.2210/pdb6eou/pdb
Descriptor	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (2 entities in total)
Functional Keywords	intellectual disability associated point mutation in o-glcnac transferase tetratricopeptide domain, transferase
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	43540.25
Authors	Gundogdu, M.,van Aalten, D.M.F. (deposition date: 2017-10-10, release date: 2018-05-09, Last modification date: 2024-01-17)
Primary citation	Gundogdu, M.,Llabres, S.,Gorelik, A.,Ferenbach, A.T.,Zachariae, U.,van Aalten, D.M.F. The O-GlcNAc Transferase Intellectual Disability Mutation L254F Distorts the TPR Helix. Cell Chem Biol, 25:513-518.e4, 2018 Cited by PubMed Abstract: O-linked β-N-acetyl--glucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential post-translational modification that is abundant in the brain. Recently, OGT mutations have been associated with intellectual disability, although it is not understood how they affect OGT structure and function. Using a multi-disciplinary approach we show that the L254F OGT mutation leads to conformational changes of the tetratricopeptide repeats and reduced activity, revealing the molecular mechanisms contributing to pathogenesis. PubMed: 29606577 DOI: 10.1016/j.chembiol.2018.03.004 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation