1OIV

X-ray structure of the small G protein Rab11a in complex with GDP

1OIV の概要

• エントリーDOI: 10.2210/pdb1oiv/pdb
• 関連するPDBエントリー: 1OIW 1OIX
• 分子名称: RAS-RELATED PROTEIN RAB-11A, GUANOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: protein transport, small g protein, intracellular trafficking, gtp-binding, lipoprotein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44124.99

構造登録者

Pasqualato, S.,Senic-Matuglia, F.,Renault, L.,Goud, B.,Salamero, J.,Cherfils, J. (登録日: 2003-06-26, 公開日: 2004-01-08, 最終更新日: 2023-12-13)

主引用文献

Pasqualato, S.,Senic-Matuglia, F.,Renault, L.,Goud, B.,Salamero, J.,Cherfils, J.
The Structural Gdp/GTP Cycle of Rab11 Reveals a Novel Interface Involved in the Dynamics of Recycling Endosomes
J.Biol.Chem., 279:11480-, 2004

PubMed Abstract: The small GTP-binding protein Rab11 is an essential regulator of the dynamics of recycling endosomes. Here we report the crystallographic analysis of the GDP/GTP cycle of human Rab11a, and a structure-based mutagenesis study that identifies a novel mutant phenotype. The crystal structures show that the nucleotide-sensitive switch 1 and 2 regions differ from those of other Rab proteins. In Rab11-GDP, they contribute to a close packed symmetrical dimer, which may associate to membranes in the cell and allow Rab11 to undergo GDP/GTP cycles without recycling to the cytosol. The structure of active Rab11 delineates a three-dimensional site that includes switch 1 and is separate from the site defined by the Rab3/Rabphilin interface. It is proposed to form a novel interface for a Rab11 partner compatible with the simultaneous binding of another partner at the Rabphilin interface. Mutation of Ser(29) to Phe in this epitope resulted in morphological modifications of the recycling compartment that are distinct from those induced by the classical dominant-negative and constitutively active Rab11 mutants. Recycling endosomes condensed in the perinuclear region where they retained recycling transferrin, and they clustered Rab11- and EEA1-positive membranes. Altogether, our study suggests that this mutation impairs a specific subset of Rab11 interactions, possibly those involved in cytoskeleton-based movements driving the slow recycling pathway.

PubMed: 14699104
DOI: 10.1074/JBC.M310558200

実験手法

X-RAY DIFFRACTION (1.98 Å)