TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
Article Abstract:
Crystallographic, mutational and functional analyses of complexes between Rab GTPases and the TBC (Tre-2, Bub2 and Cdc16) domain of Gyp1p, a GTPase-activating protein (GAP) are reported. The TBC domain of a TBC-domain-Rab-GTPase-aluminium fluoride complex, which approximates the transition-state intermediate for GTP hydrolysis, supplies two residues, an arginine and a glutamine finger, whose strong conservation indicates that most TBC-domain GAPs may accelerate GTP hydrolysis by a dual-finger mechanism.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Structural basis of family-wide Rab GtPase recognition by rabenosyn-5
Article Abstract:
The specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family is determined. The results demonstrate that even the structurally similar effectors domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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Legionella pneumophila proteins that regulate Rab1 membrane cycling
Article Abstract:
The functions of the Legionella pneumophila proteins that control the Rab1 activity are explained. The protein is found to regulate the Rab1 membrane cycling by redirecting it to the pathogen-occupied vacuole.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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