EC Number   |
Reference |
|---|
   2.4.1.255 | - |
694327, 723250 |
| 2.4.1.255 | a binary complex with UDP and a ternary complex with UDP and peptide substrate YPGGSTPVSSANMM, hanging drop vapor diffusion method |
723266 |
| 2.4.1.255 | cocrystallization of identified substrate peptides with OGT, derived from retinoblastoma-like protein 2 (RBL2411-422, KENPAVTPVSTA), proto-oncogene tyrosine protein kinase receptor Ret (Ret660-672, AQAFPVSYSSSGA), keratin-7 (KER77-19, SPVFTSRSAAFSC) and lamin B1 (LAMIN179-191, KLSPSPSSRVTVS). The peptide is tethered into a common binding mode by a combination of van der Waals interactions and hydrogen bonds that restrict torsional freedom in the -3 to +2 subsites only |
736868 |
| 2.4.1.255 | hybrid quantum mechanics/molecular mechanics analysis of reaction paths using alpha-phosphate and Asp554 as the catalytic bases. The mechanism with alpha-phosphate acting as the base is favorable. The reaction has a rate-limiting free energy barrier of 23.5 kcal/mol, whereas reactions utilizing Asp554 and water-assisted alpha-phosphate have barriers of 41.7 and 40.9 kcal/mol, respectively |
736684 |
| 2.4.1.255 | in complex with inhibitor goblin1, to 3.15 A resolution. UDP adopts the same conformation as observed in the OGT Michaelis complex and the peptide occupies the -4 to +2 subsites with a similar backbone conformation. The three-carbon linker connects the two components without introducing any strain, allowing both the UDP moiety and the peptide part of the inhibitor to adopt the optimal position in the binding site, mimicking the natural substrates |
735633 |
| 2.4.1.255 | in complex with UDP and GlcNAc. GtfA reveals a beta-meander add-on domain beyond the catalytic domain, which is distinct from the all-alpha-tetratricopeptide repeats in the two structure-known OGTs. This add-on domain contributes to forming an active GtfA-GtfB complex and recognizing the acceptor protein |
736452 |
| 2.4.1.255 | N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D135), crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc, to 2.7 A resolution. The enzyme adopts the canonical OGT fold with the bilobal arrangement of two Rossmann-like domains, as well as the additional TPR-like helices (535566) in the N-terminal of the catalytic domain. As a result, the TPRs are in close association with the glycosyltransferase domain and the catalytic site is aligned with the channel along the main axis of the TPR superhelix |
736927 |
| 2.4.1.255 | three-dimensional structure of the protein domains I and II, conserved amino acid sequences |
489612 |
| 2.4.1.255 | vapour diffusion crystallisation experiments are performed |
707093, 707095 |
| 2.4.1.255 | X-ray crystallography |
692070 |
