Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Akutsu M,Kawasaki M,Katoh Y,Shiba T,Yamaguchi Y,Kato R,Kato K,Nakayama K,Wakatsuki S

doi

10.1016/j.febslet.2005.08.076

keywords:

subject

Has Abstract

pub_date

2005-10-10 00:00:00

pages

5385-91

issue

24

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)01100-2

journal_volume

579

pub_type

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