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4UJ5

Crystal structure of human Rab11-Rabin8-FIP3

Summary for 4UJ5
Entry DOI10.2210/pdb4uj5/pdb
Related4UJ3 4UJ4
DescriptorRAS-RELATED PROTEIN RAB-11A, RAB-3A-INTERACTING PROTEIN, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (6 entities in total)
Functional Keywordstransport protein, ciliary targeting complex, cilium, vesicu transport, membrane trafficking, rabin8, rab11, fip3
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationCell membrane; Peripheral membrane protein: P62491
Cytoplasm: Q96QF0
Total number of polymer chains4
Total formula weight87312.93
Authors
Vetter, M.,Lorentzen, E. (deposition date: 2015-04-08, release date: 2015-08-12, Last modification date: 2024-01-10)
Primary citationVetter, M.,Stehle, R.,Basquin, C.,Lorentzen, E.
Structure of Rab11-Fip3-Rabin8 Reveals Simultaneous Binding of Fip3 and Rabin8 Effectors to Rab11.
Nat.Struct.Mol.Biol., 22:695-, 2015
Cited by
PubMed Abstract: The small GTPase Rab11 and its effectors FIP3 and Rabin8 are essential to membrane-trafficking pathways required for cytokinesis and ciliogenesis. Although effector binding is generally assumed to be sequential and mutually exclusive, we show that Rab11 can simultaneously bind FIP3 and Rabin8. We determined crystal structures of human Rab11-GMPPNP-Rabin8 and Rab11-GMPPNP-FIP3-Rabin8. The structures reveal that the C-terminal domain of Rabin8 adopts a previously undescribed fold that interacts with Rab11 at an unusual effector-binding site neighboring the canonical FIP3-binding site. We show that Rab11-GMPPNP-FIP3-Rabin8 is more stable than Rab11-GMPPNP-Rabin8, owing to direct interaction between Rabin8 and FIP3 within the dual effector-bound complex. The data allow us to propose a model for how membrane-targeting complexes assemble at the trans-Golgi network and recycling endosomes, through multiple weak interactions that create high-avidity complexes.
PubMed: 26258637
DOI: 10.1038/NSMB.3065
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.604 Å)
Structure validation

226707

数据于2024-10-30公开中

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