Structure of the GAT domain of the endosomal Q2 adapter protein Tom1

July 28, 2017

Title

Structure of the GAT domain of the endosomal Q2 adapter protein Tom1

Author

Shuyan Xiao, Jeffrey F. Ellena, Geoffrey S. Armstrong, Daniel G.S. Capelluto

Year

2016

Journal

Data in Brief

Abstract

Cellular homeostasis requires correct delivery of cell-surface receptor proteins (cargo) to their target subcellular compartments. The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments. Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD). In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain. The estimated protein structure exhibits a bundle of three helical elements. We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Biochemistry