1T91

crystal structure of human small GTPase Rab7(GTP)

1T91 の概要

• エントリーDOI: 10.2210/pdb1t91/pdb
• 分子名称: Ras-related protein Rab-7, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: protein transport, small gtpase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Late endosome: P51149
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96196.93

構造登録者

Song, H.,Hong, W.,Wu, M.,Wang, T. (登録日: 2004-05-14, 公開日: 2005-05-17, 最終更新日: 2023-10-25)

主引用文献

Wu, M.,Wang, T.,Loh, E.,Hong, W.,Song, H.
Structural basis for recruitment of RILP by small GTPase Rab7.
Embo J., 24:1491-1501, 2005

PubMed Abstract: Rab7 regulates vesicle traffic from early to late endosomes, and from late endosomes to lysosomes. The crystal structure of Rab7-GTP in complex with the Rab7 binding domain of RILP reveals that Rab7 interacts with RILP specifically via two distinct areas, with the first one involving the switch and interswitch regions and the second one consisting of RabSF1 and RabSF4. Disruption of these interactions by mutations abrogates late endosomal/lysosomal targeting of Rab7 and RILP. The Rab7 binding domain of RILP forms a coiled-coil homodimer with two symmetric surfaces to interact with two separate Rab7-GTP molecules, forming a dyad configuration of Rab7-RILP(2)-Rab7. Mutations that disrupt RILP dimerization also abolish its interactions with Rab7-GTP and late endosomal/lysosomal targeting, suggesting that the dimeric form of RILP is a functional unit. Structural comparison suggests that the combined use of RabSF1 and RabSF4 with the switch regions may be a general mode of action for most Rab proteins in regulating membrane trafficking.

PubMed: 15933719
DOI: 10.1038/sj.emboj.7600643

実験手法

X-RAY DIFFRACTION (1.9 Å)