Structural snapshots of the reaction coordinate for O-GlcNAc transferase

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Structural snapshots of the reaction coordinate for O-GlcNAc transferase

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Title: Structural snapshots of the reaction coordinate for O-GlcNAc transferase
Author: Lazarus, Michael B.; Jiang, Jiaoyang; Gloster, Tracey M.; Zandberg, Wesley F.; Whitworth, Garrett E.; Vocadlo, David J.; Walker, Suzanne

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Citation: Lazarus, Michael B., Jiaoyang Jiang, Tracey M. Gloster, Wesley F. Zandberg, Garrett E. Whitworth, David J. Vocadlo, and Suzanne Walker. 2012. “Structural snapshots of the reaction coordinate for O-GlcNAc transferase.” Nature chemical biology 8 (12): 966-968. doi:10.1038/nchembio.1109. http://dx.doi.org/10.1038/nchembio.1109.
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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-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.
Published Version: doi:10.1038/nchembio.1109
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3508357/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:11708547
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