Structure of the GAT domain of the endosomal adapter protein Tom1

Structure of the GAT domain of the endosomal adapter protein Tom1

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 media...

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Main Authors: Shuyan Xiao, Jeffrey F. Ellena, Geoffrey S. Armstrong, Daniel G.S. Capelluto
Format: Article
Language:English
Published: Elsevier 2016-06-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340916300646
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spelling doaj-8c637436e91a4883a6b8b52f2e03d7792020-11-25T01:28:35ZengElsevierData in Brief2352-34092016-06-017344348Structure of the GAT domain of the endosomal adapter protein Tom1Shuyan Xiao0Jeffrey F. Ellena1Geoffrey S. Armstrong2Daniel G.S. Capelluto3Protein Signaling Domains Laboratory, Department of Biological Sciences, Biocomplexity Institute, Virginia Tech, Blacksburg, VA 24061, USA; School of Materials and Metallurgy, Inner Mongolia University of Science and Technology, PR ChinaDepartment of Chemistry and Biochemistry, University of Virginia, Charlottesville, VA 22904, USADepartments of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USAProtein Signaling Domains Laboratory, Department of Biological Sciences, Biocomplexity Institute, Virginia Tech, Blacksburg, VA 24061, USA; Corresponding author.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. Keywords: Tom1, GAT domain, Tollip, Ubiquitin, nuclear magnetic resonancehttp://www.sciencedirect.com/science/article/pii/S2352340916300646
collection DOAJ
language English
format Article
sources DOAJ
author Shuyan Xiao
Jeffrey F. Ellena
Geoffrey S. Armstrong
Daniel G.S. Capelluto
spellingShingle Shuyan Xiao
Jeffrey F. Ellena
Geoffrey S. Armstrong
Daniel G.S. Capelluto
Structure of the GAT domain of the endosomal adapter protein Tom1
Data in Brief
author_facet Shuyan Xiao
Jeffrey F. Ellena
Geoffrey S. Armstrong
Daniel G.S. Capelluto
author_sort Shuyan Xiao
title Structure of the GAT domain of the endosomal adapter protein Tom1
title_short Structure of the GAT domain of the endosomal adapter protein Tom1
title_full Structure of the GAT domain of the endosomal adapter protein Tom1
title_fullStr Structure of the GAT domain of the endosomal adapter protein Tom1
title_full_unstemmed Structure of the GAT domain of the endosomal adapter protein Tom1
title_sort structure of the gat domain of the endosomal adapter protein tom1
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2016-06-01
description 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. Keywords: Tom1, GAT domain, Tollip, Ubiquitin, nuclear magnetic resonance
url http://www.sciencedirect.com/science/article/pii/S2352340916300646
work_keys_str_mv AT shuyanxiao structureofthegatdomainoftheendosomaladapterproteintom1
AT jeffreyfellena structureofthegatdomainoftheendosomaladapterproteintom1
AT geoffreysarmstrong structureofthegatdomainoftheendosomaladapterproteintom1
AT danielgscapelluto structureofthegatdomainoftheendosomaladapterproteintom1
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