1WRD

Crystal structure of Tom1 GAT domain in complex with ubiquitin

Summary for 1WRD

• Entry DOI: 10.2210/pdb1wrd/pdb
• Descriptor: Target of Myb protein 1, Ubiquitin (3 entities in total)
• Functional Keywords: three-helix bundle, ubiquitin-binding protein, protein transport-signaling protein complex, protein transport/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (Probable): O60784
• Total number of polymer chains: 2
• Total formula weight: 20379.28

Authors

Akutsu, M.,Kawasaki, M.,Katoh, Y.,Shiba, T.,Yamaguchi, Y.,Kato, R.,Kato, K.,Nakayama, K.,Wakatsuki, S. (deposition date: 2004-10-14, release date: 2005-10-11, Last modification date: 2024-03-13)

Primary citation

Akutsu, M.,Kawasaki, M.,Katoh, Y.,Shiba, T.,Yamaguchi, Y.,Kato, R.,Kato, K.,Nakayama, K.,Wakatsuki, S.
Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain.
Febs Lett., 579:5385-5391, 2005

PubMed Abstract: 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.

PubMed: 16199040
DOI: 10.1016/j.febslet.2005.08.076

Experimental method

X-RAY DIFFRACTION (1.75 Å)