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Structure and mutational analysis of Rab GDP-dissociation inhibitor

Nature volume 381, pages 42–48 (1996)Cite this article

Abstract

The crystal structure of the bovine α-isoform of Rab GDP-dissociation inhibitor (GDI), which functions in vesicle-membrane transport to recycle and regulate Rab GTPases, has been determined to a resolution of 1.81 Å. GDI is constructed of two main structural units, a large complex multisheet domain I and a smaller α-helical domain II. The structural organization of domain I is surprisingly closely related to FAD-containing monooxygenases and oxidases. Sequence-conserved regions common to GDI and the choroideraemia gene product, which delivers Rab to catalytic subunits of Rab geranylgeranyltransferase II, are clustered on one face of the molecule. The two most sequence-conserved regions, which form a compact structure at the apex of GDI, are shown by site-directed mutagenesis to play a critical role in the binding of Rab proteins.

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Author notes

  1. Isabella Schalk

    Present address: Laboratoire de Chimie Microbienne, Institut de Chimie, BP 296 R/8, 1 rue Blaise Pascal, 67008, Strasbourg Cedex, France

Authors and Affiliations

  1. Department of Molecular, The Scripps Research Institute, 10666 N. Torrey Pines Road, La Jolla, California, 92037, USA

    Isabella Schalk, Ke Zeng, Enrico A. Stura, Mingdong Huang & Ian A. Wilson

  2. Department of Cell Biology, The Scripps Research Institute, 10666 N. Torrey Pines Road, La Jolla, California, 92037, USA

    Isabella Schalk, Ke Zeng, Shih-Kwang Wu, Jeanne Matteson, Anurag Tandon & William E. Balch

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Schalk, I., Zeng, K., Wu, SK. et al. Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 381, 42–48 (1996). https://doi.org/10.1038/381042a0

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