7YH2
TRAPPC3 from Thorarchaeota AB25
Summary for 7YH2
Entry DOI | 10.2210/pdb7yh2/pdb |
Descriptor | TRAPPC3 from Thorarchaeota AB25, ZINC ION (3 entities in total) |
Functional Keywords | asgard archaea, trapp, unknown function |
Biological source | Candidatus Thorarchaeota archaeon AB_25 |
Total number of polymer chains | 2 |
Total formula weight | 36390.29 |
Authors | Robinson, R.C.,Tran, L.T. (deposition date: 2022-07-12, release date: 2023-07-19, Last modification date: 2025-01-29) |
Primary citation | Tran, L.T.,Akil, C.,Senju, Y.,Robinson, R.C. The eukaryotic-like characteristics of small GTPase, roadblock and TRAPPC3 proteins from Asgard archaea. Commun Biol, 7:273-273, 2024 Cited by PubMed Abstract: Membrane-enclosed organelles are defining features of eukaryotes in distinguishing these organisms from prokaryotes. Specification of distinct membranes is critical to assemble and maintain discrete compartments. Small GTPases and their regulators are the signaling molecules that drive membrane-modifying machineries to the desired location. These signaling molecules include Rab and Rag GTPases, roadblock and longin domain proteins, and TRAPPC3-like proteins. Here, we take a structural approach to assess the relatedness of these eukaryotic-like proteins in Asgard archaea, the closest known prokaryotic relatives to eukaryotes. We find that the Asgard archaea GTPase core domains closely resemble eukaryotic Rabs and Rags. Asgard archaea roadblock, longin and TRAPPC3 domain-containing proteins form dimers similar to those found in the eukaryotic TRAPP and Ragulator complexes. We conclude that the emergence of these protein architectures predated eukaryogenesis, however further adaptations occurred in proto-eukaryotes to allow these proteins to regulate distinct internal membranes. PubMed: 38472392DOI: 10.1038/s42003-024-05888-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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