1wrd
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrd OCA], [http://www.ebi.ac.uk/pdbsum/1wrd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wrd RCSB]</span> | ||
}} | }} | ||
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[[Category: ubiquitin-binding protein]] | [[Category: ubiquitin-binding protein]] | ||
| - | ''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 00:40:01 2008'' |
Revision as of 21:40, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Tom1 GAT domain in complex with ubiquitin
Overview
Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices alpha1 and alpha2. NMR and biochemical data revealed that the N-terminal half of helix alpha3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.
About this Structure
1WRD is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain., Akutsu M, Kawasaki M, Katoh Y, Shiba T, Yamaguchi Y, Kato R, Kato K, Nakayama K, Wakatsuki S, FEBS Lett. 2005 Oct 10;579(24):5385-91. PMID:16199040
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