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2HV8

Crystal structure of GTP-bound Rab11 in complex with FIP3

Summary for 2HV8
Entry DOI10.2210/pdb2hv8/pdb
DescriptorRas-related protein Rab-11A, Rab11 family-interacting protein 3, MAGNESIUM ION, ... (8 entities in total)
Functional Keywordsprotein transport, rab11a, fip3, cytokinesis, recycling endosomes
Biological sourceHomo sapiens (human)
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Cellular locationCell membrane; Peripheral membrane protein: P62491
Recycling endosome membrane; Peripheral membrane protein: O75154
Total number of polymer chains6
Total formula weight81820.52
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 citationEathiraj, 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: 17007872
DOI: 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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