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

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.

SUBMITTER: Xiao S

PROVIDER: S-EPMC4781976 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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

Xiao Shuyan S Ellena Jeffrey F JF Armstrong Geoffrey S GS Capelluto Daniel G S DG

Data in brief 20160224

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 ex ...[more]

PMID: 26977434

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