Crystal structure of the Rab-binding domain of Rab11 family-interacting protein 2

The small GTPases Rab11, Rab14 and Rab25 regulate membrane trafficking through the recruitment of Rab11 family-interacting proteins (FIPs) to endocytic compartments. FIPs are multi-domain effector proteins that have a highly conserved Rab-binding domain (RBD) at their C-termini. Several structures of complexes of Rab11 with RBDs have previously been determined, including those of Rab11 – FIP2 and Rab11 – FIP3. In addition, the structures of the Rab14 – FIP1 and Rab25 – FIP2 complexes have been determined. All of the RBD structures contain a central parallel coiled coil in the RBD that binds to the switch 1 and switch 2 regions of the Rab. Here, the crystal structure of the uncomplexed RBD of FIP2 is presented at 2.3   Å resolution. The structure reveals antiparallel α -helices that associate through polar interactions. These include a remarkable stack of arginine residues within a four-helix bundle in the crystal lattice.

Source: Acta Crystallographica Section F - July 27, 2020 Category: Biochemistry Authors: Kearney, A.M. Khan, A.R. Tags: Rab11 family-interacting protein 2 ab initio phasing Rab-binding domain GTPases research communications Source Type: research