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PDBsum entry 2k5u
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Signaling protein
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PDB id
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2k5u
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References listed in PDB file
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Key reference
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Title
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Structure and membrane interaction of myristoylated arf1.
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Authors
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Y.Liu,
R.A.Kahn,
J.H.Prestegard.
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Ref.
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Structure, 2009,
17,
79-87.
[DOI no: ]
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PubMed id
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Abstract
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ADP-ribosylation factors (ARFs) are small (21 kDa), monomeric GTPases that are
important regulators of membrane traffic. When membrane bound, they recruit
soluble adaptors to membranes and trigger the assembly of coating complexes
involved in cargo selection and vesicular budding. N-myristoylation is a
conserved feature of all ARF proteins that is required for its biological
functions, although the mechanism(s) by which the myristate acts in ARF
functions is not fully understood. Here we present the structure of a
myristoylated ARF1 protein, determined by solution NMR methods, and an
assessment of the influence of myristoylation on association of ARF1.GDP and
ARF1.GTP with lipid bilayers. A model in which myristoylation contributes to
both the regulation of guanine nucleotide exchange and stable membrane
association is supported.
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Figure 1.
Figure 1. ^15N-^1H HSQC Spectra of myr(+)- and
myr(−)-yARF1·GDP
myr(+)- and
myr(−)-yARF1·GDP are shown in blue and red,
respectively. Blown-up views of chemical shift perturbed
residues are displayed on the bottom.
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Figure 2.
Figure 2. Structure of Myristoylated yARF1 and Comparisons to
Related Structures
(A) Overlap of 15 accepted
myr(+)-yARF1·GDP structures out of 100 trials. GDP is
shown in blue and myristoyl is in purple.
(B) The myristoyl
binding pocket with leucines shown in red, isoleucines in blue,
tyrosines in cyan, and myristoyl in purple.
(C) The
myristoyl binding pocket lies under the N-terminal amphiphilic
helix in the myr(−)-hARF·GDP structure (Protein Data
Bank ID code 1hur).
(D) The interstrand loop λ3 clashes
with the myristoyl chain in the GTP-bound conformation but not
in the GDP-bound conformation. The backbone of
myr(+)-yARF1·GDP is shown in ivory,
myr(−)-hARF1·GDP in blue, and hARF1Δ17·GTP in
green. λ3 of all molecules is shown in red, and myristoyl is
shown in purple.
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The above figures are
reprinted
from an Open Access publication published by Cell Press:
Structure
(2009,
17,
79-87)
copyright 2009.
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