2HV8
Crystal structure of GTP-bound Rab11 in complex with FIP3
Summary for 2HV8
Entry DOI | 10.2210/pdb2hv8/pdb |
Descriptor | Ras-related protein Rab-11A, Rab11 family-interacting protein 3, MAGNESIUM ION, ... (8 entities in total) |
Functional Keywords | protein transport, rab11a, fip3, cytokinesis, recycling endosomes |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane; Peripheral membrane protein: P62491 Recycling endosome membrane; Peripheral membrane protein: O75154 |
Total number of polymer chains | 6 |
Total formula weight | 81820.52 |
Authors | Eathiraj, S.,Mishra, A.,Prekeris, R.,Lambright, D.G. (deposition date: 2006-07-27, release date: 2006-11-21, Last modification date: 2023-08-30) |
Primary citation | Eathiraj, S.,Mishra, A.,Prekeris, R.,Lambright, D.G. Structural Basis for Rab11-mediated Recruitment of FIP3 to Recycling Endosomes. J.Mol.Biol., 364:121-135, 2006 Cited by PubMed Abstract: The Rab11 GTPase regulates recycling of internalized plasma membrane receptors and is essential for completion of cytokinesis. A family of Rab11 interacting proteins (FIPs) that conserve a C-terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. Normal completion of cytokinesis requires a complex between Rab11 and FIP3. Here, we report the crystal structure and mutational analysis of a heterotetrameric complex between constitutively active Rab11 and a FIP3 construct that includes the RBD. Two Rab11 molecules bind to dyad symmetric sites at the C terminus of FIP3, which forms a non-canonical coiled-coiled dimer with a flared C terminus and hook region. The RBD overlaps with the coiled coil and extends through the C-terminal hook. Although FIP3 engages the switch and interswitch regions of Rab11, the mode of interaction differs significantly from that of other Rab-effector complexes. In particular, the switch II region undergoes a large structural rearrangement from an ordered but non-complementary active conformation to a remodeled conformation that facilitates the interaction with FIP3. Finally, we provide evidence that FIP3 can form homo-oligomers in cells, and that a critical determinant of Rab11 binding in vitro is necessary for FIP3 recruitment to recycling endosomes during cytokinesis. PubMed: 17007872DOI: 10.1016/j.jmb.2006.08.064 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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