1GND

GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM

Summary for 1GND

• Entry DOI: 10.2210/pdb1gnd/pdb
• Descriptor: GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR (2 entities in total)
• Functional Keywords: gtpase activation
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 50620.46

Authors

Schalk, I.,Zeng, K.,Wu, S.-K.,Stura, E.A.,Metteson, J.,Huang, M.,Tandon, A.,Wilson, I.A.,Balch, W.E. (deposition date: 1996-07-10, release date: 1997-02-12, Last modification date: 2024-02-07)

Primary citation

Schalk, I.,Zeng, K.,Wu, S.K.,Stura, E.A.,Matteson, J.,Huang, M.,Tandon, A.,Wilson, I.A.,Balch, W.E.
Structure and mutational analysis of Rab GDP-dissociation inhibitor.
Nature, 381:42-48, 1996

PubMed Abstract: The crystal structure of the bovine alpha-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 A. GDI is constructed of two main structural units, a large complex multisheet domain I and a smaller alpha-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.

PubMed: 8609986
DOI: 10.1038/381042a0

Experimental method

X-RAY DIFFRACTION (1.81 Å)