LepB operates by a different catalytic mechanism compared with classical RabGAPs. LepB operates by a different catalytic mechanism compared with classical.

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LepB operates by a different catalytic mechanism compared with classical RabGAPs. LepB operates by a different catalytic mechanism compared with classical RabGAPs. (A) Cartoon representation of the crystal structure of the complex between Rab1b3–174, LepB317–618 (SER‐mutant), GDP and BeF3 (grey, orange: N‐ and C‐terminal subdomains of the LepB GAP domain; green: Rab1b3–174 with switch I (purple), switch II (yellow) and P‐loop (blue)). (B) Interactions between GDP, BeF3, Mg2+, Rab1b3–174 and LepB317–618 in the nucleotide‐binding pocket. LepB provides an arginine finger (R444L) that is involved in GTP hydrolysis. The structure suggests that Rab glutamine Q67R is also involved in catalysis, which is mechanistically different from TBC‐domain‐containing proteins. (C) GTP‐hydrolysis kinetics of 0.5 μM Rab1bwt catalyzed by 2.5 μM LepB299–618 and 2.5 μM LepB299–618 R444A monitored by the change of Rab1b tryptophan fluorescence, demonstrating the significance of the arginine finger R444L of LepB for GAP activity. (D) The cis‐glutamine of Rab1b is important for GTP hydrolysis by LepB, but not TBC1D20. The figures compares the catalytic activities (kcat/KM) of LepB and TBC1D20 in dependence of wild‐type and the Q67A mutant of Rab1. The Q67R substitution affects catalysis by LepB (14,400 × reduction) 293 times more severly than for TBC1D20 (49 × reduction). GAP, GTPase‐activating protein. Emerich Mihai Gazdag et al. EMBO Rep. 2013;14:199-205 © as stated in the article, figure or figure legend