2GZD

Crystal Structure of Rab11 in Complex with Rab11-FIP2

Summary for 2GZD

• Entry DOI: 10.2210/pdb2gzd/pdb
• Descriptor: Ras-related protein Rab-11A, Rab11 family-interacting protein 2, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: g protein folds, a-helical coiled coil, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Peripheral membrane protein: P62491 Q7L804
• Total number of polymer chains: 4
• Total formula weight: 64864.25

Authors

Khan, A.R. (deposition date: 2006-05-11, release date: 2006-08-15, Last modification date: 2024-11-06)

Primary citation

Jagoe, W.N.,Lindsay, A.J.,Read, R.J.,McCoy, A.J.,McCaffrey, M.W.,Khan, A.R.
Crystal structure of rab11 in complex with rab11 family interacting protein 2.
Structure, 14:1273-1283, 2006

PubMed Abstract: 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.

PubMed: 16905101
DOI: 10.1016/j.str.2006.06.010

Experimental method

X-RAY DIFFRACTION (2.44 Å)