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PDBsum entry 3n5c
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Protein transport
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PDB id
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3n5c
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References listed in PDB file
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Key reference
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Title
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Saxs and x-Ray crystallography suggest an unfolding model for the gdp/gtp conformational switch of the small gtpase arf6.
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Authors
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V.Biou,
K.Aizel,
P.Roblin,
A.Thureau,
E.Jacquet,
S.Hansson,
B.Guibert,
E.Guittet,
C.Van heijenoort,
M.Zeghouf,
J.Perez,
J.Cherfils.
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Ref.
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J Mol Biol, 2010,
402,
696-707.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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The small GTPases Arf1 and Arf6 have nonoverlapping functions in cellular
traffic despite their very high sequence and structural resemblance. Notably,
the exquisite isoform specificity of their guanine nucleotide exchange factors
and their distinctive sensitivity to the drug brefeldin A cannot be explained by
any straightforward structural model. Here we integrated structural and
spectroscopic methods to address this issue using Δ13Arf6-GDP, a truncated
mutant that mimics membrane-bound Arf6-GDP. The crystal structure of
Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands,
which is fully accounted for by small-angle X-ray scattering data in solution
and by ab initio three-dimensional envelope calculation. NMR chemical shifts
identify this structural disorder in Δ13Arf6-GDP, but not in the closely
related Δ17Arf1-GDP, which is consistent with their comparative thermodynamic
and hydrodynamic analyses. Taken together, these experiments suggest an
unfolding model for the nucleotide switch of Arf6 and shed new light on its
biochemical differences with Arf1.
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