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PDBsum entry 1d5t
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Hydrolase inhibitor
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PDB id
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1d5t
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A new functional domain of guanine nucleotide dissociation inhibitor (alpha-Gdi) involved in rab recycling.
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Authors
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P.Luan,
A.Heine,
K.Zeng,
B.Moyer,
S.E.Greasely,
P.Kuhn,
W.E.Balch,
I.A.Wilson.
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Ref.
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Traffic, 2000,
1,
270-281.
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PubMed id
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Abstract
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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.
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