1D5T

GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM

Summary for 1D5T

• Entry DOI: 10.2210/pdb1d5t/pdb
• Related: 1gnd
• Descriptor: GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase inhibitor
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm : P21856
• Total number of polymer chains: 1
• Total formula weight: 49122.77

Authors

Peng, L.,Zeng, K.,Heine, A.,Moyer, B.,Greasley, S.E.,Kuhn, P.,Balch, W.E.,Wilson, I.A. (deposition date: 1999-10-11, release date: 2000-10-25, Last modification date: 2023-08-09)

Primary citation

Luan, P.,Heine, A.,Zeng, K.,Moyer, B.,Greasely, S.E.,Kuhn, P.,Balch, W.E.,Wilson, I.A.
A new functional domain of guanine nucleotide dissociation inhibitor (alpha-GDI) involved in Rab recycling.
Traffic, 1:270-281, 2000

PubMed Abstract: Guanine nucleotide dissociation inhibitor (GDI) is a 55-kDa protein that functions in vesicular membrane transport to recycle Rab GTPases. We have now determined the crystal structure of bovine alpha-GDI at ultra-high resolution (1.04 A). Refinement at this resolution highlighted a region with high mobility of its main-chain residues. This corresponded to a surface loop in the primarily alpha-helical domain II at the base of alpha-GDI containing the previously uncharacterized sequence-conserved region (SCR) 3A. Site-directed mutagenesis showed that this mobile loop plays a crucial role in binding of GDI to membranes and extraction of membrane-bound Rab. This domain, referred to as the mobile effector loop, in combination with Rab-binding residues found in the multi-sheet domain I at the apex of alpha-GDI may provide flexibility for recycling of diverse Rab GTPases. We propose that conserved residues in domains I and II synergize to form the functional face of GDI, and that domain II mediates a critical step in Rab recycling during vesicle fusion.

PubMed: 11208110
DOI: 10.1034/j.1600-0854.2000.010309.x

Experimental method

X-RAY DIFFRACTION (1.04 Å)