3pe3: Difference between revisions
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[[Image:3pe3.png|left|200px]] | [[Image:3pe3.png|left|200px]] | ||
{{STRUCTURE_3pe3| PDB=3pe3 | SCENE= }} | {{STRUCTURE_3pe3| PDB=3pe3 | SCENE= }} | ||
===Structure of human O-GlcNAc transferase and its complex with a peptide substrate=== | ===Structure of human O-GlcNAc transferase and its complex with a peptide substrate=== | ||
{{ABSTRACT_PUBMED_21240259}} | {{ABSTRACT_PUBMED_21240259}} | ||
==About this Structure== | ==About this Structure== | ||
[[3pe3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PE3 OCA]. | [[3pe3]] is a 4 chain structure of [[O-GlcNAc transferase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PE3 OCA]. | ||
==See Also== | |||
*[[Human O-GlcNAc transferase|Human O-GlcNAc transferase]] | |||
*[[O-GlcNAc transferase|O-GlcNAc transferase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021240259</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Jiang, J.]] | [[Category: Jiang, J.]] | ||
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[[Category: Sliz, P.]] | [[Category: Sliz, P.]] | ||
[[Category: Walker, S.]] | [[Category: Walker, S.]] | ||
[[Category: Glycosyltransferase]] | |||
[[Category: Gt-b]] | |||
[[Category: Transferase]] | |||
Revision as of 14:13, 27 July 2012
Structure of human O-GlcNAc transferase and its complex with a peptide substrateStructure of human O-GlcNAc transferase and its complex with a peptide substrate
The essential mammalian enzyme O-linked beta-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 A resolution) and as a ternary complex with UDP and a peptide substrate (1.95 A). 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.
Structure of human O-GlcNAc transferase and its complex with a peptide substrate., Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S, Nature. 2011 Jan 27;469(7331):564-7. Epub 2011 Jan 16. PMID:21240259
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this StructureAbout this Structure
3pe3 is a 4 chain structure of O-GlcNAc transferase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature. 2011 Jan 27;469(7331):564-7. Epub 2011 Jan 16. PMID:21240259 doi:10.1038/nature09638