2N9D

Structure analysis of the Tom1 GAT domain reveals distinct ligand-specific conformational states

Summary for 2N9D

• Entry DOI: 10.2210/pdb2n9d/pdb
• NMR Information: BMRB: 26574
• Descriptor: Target of Myb protein 1 (1 entity in total)
• Functional Keywords: transport protein, tom1, early endosomes, alternative escrt-0 member, cargo
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : O60784
• Total number of polymer chains: 1
• Total formula weight: 11501.09

Authors

Xiao, S.,Jeffrey, E.F.,Geoffrey, A.S.,Capelluto, D.G.S. (deposition date: 2015-11-15, release date: 2016-09-21, Last modification date: 2024-05-01)

Primary citation

Xiao, S.,Ellena, J.F.,Armstrong, G.S.,Capelluto, D.G.
Structure of the GAT domain of the endosomal adapter protein Tom1.
Data Brief, 7:344-348, 2016

PubMed 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.

PubMed: 26977434
DOI: 10.1016/j.dib.2016.02.042

Experimental method

SOLUTION NMR