Unknown

Dataset Information

0

Structural snapshots of the reaction coordinate for O-GlcNAc transferase.


ABSTRACT: Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked ?-N-acetylglucosamine transferase (O-GlcNAc transferase), an intracellular enzyme that catalyzes installation of a dynamic post-translational modification. The structures reveal key features of the mechanism and show that substrate participation is important during catalysis.

SUBMITTER: Lazarus MB 

PROVIDER: S-EPMC3508357 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural snapshots of the reaction coordinate for O-GlcNAc transferase.

Lazarus Michael B MB   Jiang Jiaoyang J   Gloster Tracey M TM   Zandberg Wesley F WF   Whitworth Garrett E GE   Vocadlo David J DJ   Walker Suzanne S  

Nature chemical biology 20121028 12


Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase), an intracellular enzyme that catalyzes installation of a dynamic post-translational modification. The structures reveal key features of the mechani  ...[more]

Similar Datasets

| S-EPMC10913048 | biostudies-literature
| S-EPMC3975890 | biostudies-literature
| S-EPMC2556091 | biostudies-literature
| S-EPMC9136930 | biostudies-literature
| S-EPMC6948774 | biostudies-literature
| S-EPMC5588854 | biostudies-literature
| S-EPMC4120696 | biostudies-literature
| S-EPMC8037101 | biostudies-literature
| S-EPMC4840301 | biostudies-literature
| S-EPMC8626477 | biostudies-literature