7R3M
Structure in solution of the TANGO1 cargo-binding domain (21-131)
Summary for 7R3M
| Entry DOI | 10.2210/pdb7r3m/pdb |
| NMR Information | BMRB: 34708 |
| Descriptor | Transport and Golgi organization protein 1 homolog (1 entity in total) |
| Functional Keywords | er, tango1, mia3, moth domain, protein transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 12890.38 |
| Authors | Arnolds, O.,Stoll, R. (deposition date: 2022-02-07, release date: 2023-02-22, Last modification date: 2024-10-23) |
| Primary citation | Arnolds, O.,Stoll, R. Characterization of a fold in TANGO1 evolved from SH3 domains for the export of bulky cargos. Nat Commun, 14:2273-2273, 2023 Cited by PubMed Abstract: Bulky cargos like procollagens, apolipoproteins, and mucins exceed the size of conventional COPII vesicles. During evolution a process emerged in metazoans, predominantly governed by the TANGO1 protein family, that organizes cargo at the exit sites of the endoplasmic reticulum and facilitates export by the formation of tunnel-like connections between the ER and Golgi. Hitherto, cargo-recognition appeared to be mediated by an SH3-like domain. Based on structural and dynamic data as well as interaction studies from NMR spectroscopy and microscale thermophoresis presented here, we show that the luminal cargo-recognition domain of TANGO1 adopts a new functional fold for which we suggest the term MOTH (MIA, Otoraplin, TALI/TANGO1 homology) domain. These MOTH domains, as well as an evolutionary intermediate found in invertebrates, constitute a distinct domain family that emerged from SH3 domains and acquired the ability to bind collagen. PubMed: 37080980DOI: 10.1038/s41467-023-37705-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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