1w3b
From Proteopedia
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|PDB= 1w3b |SIZE=350|CAPTION= <scene name='initialview01'>1w3b</scene>, resolution 2.85Å | |PDB= 1w3b |SIZE=350|CAPTION= <scene name='initialview01'>1w3b</scene>, resolution 2.85Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3b OCA], [http://www.ebi.ac.uk/pdbsum/1w3b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w3b RCSB]</span> | ||
}} | }} | ||
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[[Category: Lazarus, B D.]] | [[Category: Lazarus, B D.]] | ||
[[Category: Rehwinkel, J.]] | [[Category: Rehwinkel, J.]] | ||
| - | [[Category: CA]] | ||
[[Category: glcnac]] | [[Category: glcnac]] | ||
[[Category: nucleoporin]] | [[Category: nucleoporin]] | ||
| Line 38: | Line 40: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:34 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 2.85Å | |||||||
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| 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.
Overview
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.
About this Structure
1W3B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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