2D7C

Crystal structure of human Rab11 in complex with FIP3 Rab-binding domain

Summary for 2D7C

• Entry DOI: 10.2210/pdb2d7c/pdb
• Descriptor: Ras-related protein Rab-11A, Rab11 family-interacting protein 3, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: gtp-ase, coiled-coil, protein transport, structural genomics
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Peripheral membrane protein: P62491; Recycling endosome membrane; Peripheral membrane protein: O75154
• Total number of polymer chains: 4
• Total formula weight: 49213.47

Authors

Shiba, T.,Koga, H.,Shin, H.W.,Kawasaki, M.,Kato, R.,Nakayama, K.,Wakatsuki, S. (deposition date: 2005-11-16, release date: 2006-09-26, Last modification date: 2024-11-13)

Primary citation

Shiba, T.,Koga, H.,Shin, H.W.,Kawasaki, M.,Kato, R.,Nakayama, K.,Wakatsuki, S.
Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.
Proc.Natl.Acad.Sci.Usa, 103:15416-15421, 2006

PubMed Abstract: Family of Rab11-interacting protein (FIP)3/Arfophlin-1 and FIP4/Arfophilin-2 are dual effectors for Rab11 and ADP ribosylation factor (ARF)5/ARF6, which are involved in membrane delivery from recycling endosomes to the plasma membrane during cytokinesis. Here, we define the distinct C-terminal binding regions of FIP3 and FIP4 for Rab11 and ARF5/ARF6. Furthermore, we determined the crystal structure of Rab11 in complex with the Rab11-binding domain (RBD) of FIP3. The long amphiphilic alpha-helix of FIP3-RBD forms a parallel coiled-coil homodimer, with two symmetric interfaces with two Rab11 molecules. The hydrophobic side of the RBD helix is involved in homodimerization and mediates the interaction with the Rab11 switch 1 region, whereas the opposite hydrophilic side interacts with the Rab11 switch 2 and is the major factor contributing to the binding specificity. The bivalent interaction of FIP3 with Rab11 at the C terminus allows FIP3 to coordinately function with other binding partners, including ARFs.

PubMed: 17030804
DOI: 10.1073/pnas.0605357103

Experimental method

X-RAY DIFFRACTION (1.75 Å)