2gzd
Crystal Structure of Rab11 in Complex with Rab11-FIP2
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OverviewOverview
The small GTPase Rab11 regulates the recycling of endosomes to the plasma, membrane via interactions with the Rab11 family of interacting proteins, (FIPs). FIPs contain a highly conserved Rab binding domain (RBD) at their, C termini whose structure is unknown. Here, we have determined the crystal, structure of the RBD of FIP2 in complex with Rab11(GTP) by single, wavelength anomalous diffraction methods. The overall structure is a, heterotetramer with dyad symmetry, arranged as a Rab11-(FIP2)2-Rab11, complex. FIP2 forms a central alpha-helical coiled coil, with both helices, contributing to the Rab11 binding patch on equivalent and opposite sides, of the homodimer. Switch 1 of Rab11 is embedded between the two helices, while switch 2 remains flexible and is peripherally associated with the, effector. The complex reveals the structural basis for Rab11 recognition, by FIPs and suggests the molecular mechanisms underlying endocytic, recycling pathways.
About this StructureAbout this Structure
2GZD is a Protein complex structure of sequences from Homo sapiens with MG and GTP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of rab11 in complex with rab11 family interacting protein 2., Jagoe WN, Lindsay AJ, Read RJ, McCoy AJ, McCaffrey MW, Khan AR, Structure. 2006 Aug;14(8):1273-83. PMID:16905101
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