1w3b

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

spinqualitylabelsall models 1w3b, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1w3b is a 2 chain structure with sequence from Human. The September 2011 RCSB PDB Molecule of the Month feature on O-GlcNAc Transferase by David Goodsell is 10.2210/rcsb_pdb/mom_2011_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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. See Also Human O-GlcNAc transferase O-GlcNAc transferase

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