The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Structure of human O-GlcNAc transferase and its complex with a peptide substrate
Open accessAbstract
The essential mammalian enzyme O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase, here OGT) couples metabolic status to the regulation of a wide variety of cellular signalling pathways by acting as a nutrient sensor. OGT catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonines of cytoplasmic, nuclear and mitochondrial proteins, including numerous transcription factors, tumour suppressors, kinases, phosphatases and histone-modifying proteins. Aberrant glycosylation by OGT has been linked to insulin resistance, diabetic complications, cancer and neurodegenerative diseases including Alzheimer’s. Despite the importance of OGT, the details of how it recognizes and glycosylates its protein substrates are largely unknown. We report here two crystal structures of human OGT, as a binary complex with UDP (2.8 Å resolution) and as a ternary complex with UDP and a peptide substrate (1.95 Å). The structures provide clues to the enzyme mechanism, show how OGT recognizes target peptide sequences, and reveal the fold of the unique domain between the two halves of the catalytic region. This information will accelerate the rational design of biological experiments to investigate OGT’s functions; it will also help the design of inhibitors for use as cellular probes and help to assess its potential as a therapeutic target.
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VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775
Essential Role of the Glycosyltransferase Sxc/Ogt in Polycomb Repression
Gambetta, M. C., Oktaba, K., & Müller, J. (2009) · Science · doi:10.1126/science.1169727 · Cited by 315
Cited by
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Chen, Q., Chen, Y., Bian, C., Fujiki, R., & Yu, X. (2013) · Nature · doi:10.1038/nature11742 · Cited by 511
linking metabolism to epigenetics through O-GlcNAcylation
Hanover, J. A., Krause, M. W., & Love, D. C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3334 · Cited by 414
A Small Molecule That Inhibits OGT Activity in Cells
Ortiz-Meoz, R. F., Jiang, J., Lazarus, M. B., Orman, M., Janetzko, J., Fan, C., Duveau, D. Y., Tan, Z.-W., Thomas, C. J., & Walker, S. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00004 · Cited by 294
Self-citationLynch, T. P., Ferrer, C. M., Jackson, S. R., Shahriari, K. S., Vosseller, K., & Reginato, M. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302547 · Cited by 286
O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains
Zhu, Y., Liu, T.-W., Cecioni, S., Eskandari, R., Zandberg, W. F., & Vocadlo, D. J. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1774 · Cited by 134
Metadata
- Authors
- Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., & Walker, S.
- Venue
- Nature
- Published
- 2011-01
- Volume
- 469
- Issue
- 7331
- Pages
- 564-567
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2050775180
- Cited by
- 458
- References
- 8
- FWCI
- 13.17
- Type
- journal article
- Language
- en
- Open access
- green
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