5SZJ

Structure of human Rab10 in complex with the bMERB domain of Mical-cL

Summary for 5SZJ

• Entry DOI: 10.2210/pdb5szj/pdb
• Descriptor: Ras-related protein Rab-10, MICAL C-terminal-like protein, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (6 entities in total)
• Functional Keywords: mical-cl, duf3585, mical, rab effector, rab10, endocytosis
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasmic vesicle membrane ; Lipid-anchor ; Cytoplasmic side : P61026; Cytoplasm : Q6ZW33
• Total number of polymer chains: 2
• Total formula weight: 41891.48

Authors

Rai, A.,Oprisko, A.,Campos, J.,Fu, Y.,Friese, T.,Itzen, A.,Goody, R.S.,Mueller, M.P.,Gazdag, E.M. (deposition date: 2016-08-14, release date: 2016-08-24, Last modification date: 2024-01-17)

Primary citation

Rai, A.,Oprisko, A.,Campos, J.,Fu, Y.,Friese, T.,Itzen, A.,Goody, R.S.,Gazdag, E.M.,Muller, M.P.
bMERB domains are bivalent Rab8 family effectors evolved by gene duplication.
Elife, 5:-, 2016

PubMed Abstract: In their active GTP-bound form, Rab proteins interact with proteins termed effector molecules. In this study, we have thoroughly characterized a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. Within our study, we show that these effectors display a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and that some of the effector domains can bind two Rab proteins via separate binding sites. Structural analysis allowed us to explain the specificity towards Rab8 family members and the presence of two similar Rab binding sites that must have evolved via gene duplication. This study is the first to thoroughly characterize a Rab effector protein that contains two separate Rab binding sites within a single domain, allowing Micals and EHBPs to bind two Rabs simultaneously, thus suggesting previously unknown functions of these effector molecules in endosomal trafficking.

PubMed: 27552051
DOI: 10.7554/eLife.18675

Experimental method

X-RAY DIFFRACTION (2.66 Å)