8A3P
Structure of human Fy-5.
Summary for 8A3P
| Entry DOI | 10.2210/pdb8a3p/pdb |
| Related | 7ND2 |
| Descriptor | Glutamine amidotransferase-like class 1 domain-containing protein 1 (1 entity in total) |
| Functional Keywords | ferry complex, rna binding, rna transport, early endosome, rna binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23321.53 |
| Authors | Schuhmacher, J.S.,Zerial, M. (deposition date: 2022-06-08, release date: 2022-06-29, Last modification date: 2024-02-07) |
| Primary citation | Quentin, D.,Schuhmacher, J.S.,Klink, B.U.,Lauer, J.,Shaikh, T.R.,Huis In 't Veld, P.J.,Welp, L.M.,Urlaub, H.,Zerial, M.,Raunser, S. Structural basis of mRNA binding by the human FERRY Rab5 effector complex. Mol.Cell, 83:1856-1871.e9, 2023 Cited by PubMed Abstract: The pentameric FERRY Rab5 effector complex is a molecular link between mRNA and early endosomes in mRNA intracellular distribution. Here, we determine the cryo-EM structure of human FERRY. It reveals a unique clamp-like architecture that bears no resemblance to any known structure of Rab effectors. A combination of functional and mutational studies reveals that while the Fy-2 C-terminal coiled-coil acts as binding region for Fy-1/3 and Rab5, both coiled-coils and Fy-5 concur to bind mRNA. Mutations causing truncations of Fy-2 in patients with neurological disorders impair Rab5 binding or FERRY complex assembly. Thus, Fy-2 serves as a binding hub connecting all five complex subunits and mediating the binding to mRNA and early endosomes via Rab5. Our study provides mechanistic insights into long-distance mRNA transport and demonstrates that the particular architecture of FERRY is closely linked to a previously undescribed mode of RNA binding, involving coiled-coil domains. PubMed: 37267906DOI: 10.1016/j.molcel.2023.05.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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