5OSH
Structure of retromer VPS29-VPS35C subunits complexed with RidL N-terminal domain (1-236)
Summary for 5OSH
| Entry DOI | 10.2210/pdb5osh/pdb |
| Descriptor | Vacuolar protein sorting-associated protein 29, Vacuolar protein sorting-associated protein 35, Interaptin (3 entities in total) |
| Functional Keywords | retromer, legionella pneumophila, transport protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 12 |
| Total formula weight | 322499.23 |
| Authors | Romano-Moreno, M.,Rojas, A.L.,Lucas, M.,Isupov, M.N.,Hierro, A. (deposition date: 2017-08-17, release date: 2017-12-13, Last modification date: 2024-05-08) |
| Primary citation | Romano-Moreno, M.,Rojas, A.L.,Williamson, C.D.,Gershlick, D.C.,Lucas, M.,Isupov, M.N.,Bonifacino, J.S.,Machner, M.P.,Hierro, A. Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL. Proc. Natl. Acad. Sci. U.S.A., 114:E11151-E11160, 2017 Cited by PubMed Abstract: Microbial pathogens employ sophisticated virulence strategies to cause infections in humans. The intracellular pathogen encodes RidL to hijack the host scaffold protein VPS29, a component of retromer and retriever complexes critical for endosomal cargo recycling. Here, we determined the crystal structure of RidL in complex with the human VPS29-VPS35 retromer subcomplex. A hairpin loop protruding from RidL inserts into a conserved pocket on VPS29 that is also used by cellular ligands, such as Tre-2/Bub2/Cdc16 domain family member 5 (TBC1D5) and VPS9-ankyrin repeat protein for VPS29 binding. Consistent with the idea of molecular mimicry in protein interactions, RidL outcompeted TBC1D5 for binding to VPS29. Furthermore, the interaction of RidL with retromer did not interfere with retromer dimerization but was essential for association of RidL with retromer-coated vacuolar and tubular endosomes. Our work thus provides structural and mechanistic evidence into how RidL is targeted to endosomal membranes. PubMed: 29229824DOI: 10.1073/pnas.1715361115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.3 Å) |
Structure validation
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