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1w3b

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1w3b, resolution 2.85Å ()
Sites:
Ligands:
Domains: TPR
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE SUPERHELICAL TPR DOMAIN OF O-LINKED GLCNAC TRANSFERASE REVEALS STRUCTURAL SIMILARITIES TO IMPORTIN ALPHA.

Publication Abstract from PubMed

Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (TPR) repeats that mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope. To gain insight into the mechanism of target recognition, we solved the crystal structure of the homodimeric TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form an elongated superhelix. The concave surface of the superhelix is lined by absolutely conserved asparagines, in a manner reminiscent of the peptide-binding site of importin alpha. Based on this structural similarity, we propose that OGT uses an analogous molecular mechanism to recognize its targets.

The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha., Jinek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, Conti E, Nat Struct Mol Biol. 2004 Oct;11(10):1001-7. Epub 2004 Sep 12. PMID:15361863

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1W3B is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Jinek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, Conti E. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nat Struct Mol Biol. 2004 Oct;11(10):1001-7. Epub 2004 Sep 12. PMID:15361863 doi:10.1038/nsmb833

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