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

ABSTRACT: 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 ?-helices that associate through polar interactions. These include a remarkable stack of arginine residues within a four-helix bundle in the crystal lattice.

SUBMITTER: Kearney AM

PROVIDER: S-EPMC7397465 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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

Kearney Aoife Mairead AM Khan Amir Rafiq AR

Acta crystallographica. Section F, Structural biology communications 20200728 Pt 8

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 determine ...[more]

PMID: 32744247

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