NDLI: Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.

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Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.

Content Provider	Semantic Scholar
Author	Itzen, Aymelt Pylypenko, Olena Goody, Roger S. Alexandrov, Kirill Rak, Alexey V.
Copyright Year	2006
Abstract	Rab GTPases function as essential regulators of vesicle transport in eukaryotic cells. MSS4 was shown to stimulate nucleotide exchange on Rab proteins associated with the exocytic pathway and to have nucleotide-free-Rab chaperone activity. A detailed kinetic analysis of MSS4 interaction with Rab8 showed that MSS4 is a relatively slow exchange factor that forms a long-lived nucleotide-free complex with RabGTPase. In contrast to other characterized exchange factor-GTPase complexes, MSS4:Rab8 complex binds GTP faster than GDP, but still ca. 3 orders of magnitude more slowly than comparable complexes. The crystal structure of the nucleotide-free MSS4:Rab8 complex revealed that MSS4 binds to the Switch I and interswitch regions of Rab8, forming an intermolecular beta-sheet. Complex formation results in dramatic structural changes of the Rab8 molecule, leading to unfolding of the nucleotide-binding site and surrounding structural elements, facilitating nucleotide release and slowing its rebinding. Coupling of nucleotide exchange activity to a cycle of GTPase unfolding and refolding represents a novel nucleotide exchange mechanism.
Starting Page	1266
Ending Page	1268
Page Count	3
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://emboj.embopress.org/content/embojnl/25/7/1445.full.pdf
PubMed reference number	16541104v1
Volume Number	25
Issue Number	7
Journal	The EMBO journal
Language	English
Access Restriction	Open
Subject Keyword	Guanine Nucleotide Exchange Factors Guanosine Diphosphate Guanosine Triphosphate Phosphohydrolases Kinetics Nucleotides PIP5K1B gene Protein Unfolding RAB8A gene RABIF gene chaperone activity orders - HL7PublishingDomain vesicle-mediated transport
Content Type	Text
Resource Type	Article

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