2hv8
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Crystal structure of GTP-bound Rab11 in complex with FIP3
OverviewOverview
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.
About this StructureAbout this Structure
2HV8 is a Protein complex structure of sequences from Homo sapiens with 2ME, MG, SO4, GTP and MES as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes., Eathiraj S, Mishra A, Prekeris R, Lambright DG, J Mol Biol. 2006 Nov 24;364(2):121-35. Epub 2006 Aug 26. PMID:17007872
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