1YHN

Structure basis of RILP recruitment by Rab7

Summary for 1YHN

• Entry DOI: 10.2210/pdb1yhn/pdb
• Related: 1T91
• Descriptor: Ras-related protein Rab-7, Rab interacting lysosomal protein, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: rilp, rab7, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Endomembrane system: Q96NA2; Late endosome: P51149
• Total number of polymer chains: 2
• Total formula weight: 31835.49

Authors

Wu, M.,Wang, T.,Hong, W.,Song, H. (deposition date: 2005-01-10, release date: 2005-05-17, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)