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PDBsum entry 2zan
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Protein transport
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PDB id
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2zan
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References listed in PDB file
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Key reference
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Title
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Nucleotide-Dependent conformational changes and assembly of the aaa atpase skd1/vps4b.
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Authors
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M.Inoue,
H.Kamikubo,
M.Kataoka,
R.Kato,
T.Yoshimori,
S.Wakatsuki,
M.Kawasaki.
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Ref.
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Traffic, 2008,
9,
2180-2189.
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PubMed id
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Abstract
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SKD1/VPS4B belongs to the adenosine triphosphatases associated with diverse
cellular activities (AAA) family and regulates multivesicular body (MVB)
biogenesis. SKD1 changes its oligomeric state during the ATPase cycle and
subsequently releases endosomal sorting complex required for transport (ESCRT)
complexes from endosomes during the formation of MVBs. In this study, we
describe domain motions in monomeric SKD1 on ATP and ADP binding. Nucleotides
bind between the alpha/beta and the alpha-helical domains of SKD1, inducing a
approximately 20 degrees domain rotation and closure of the binding site, which
are similar to the changes observed in the AAA+ ATPase, HslU. Gel filtration and
small-angle X-ray scattering experiments showed that the ATP-bound form of SKD1
oligomerizes in solution, whereas ADP-bound and apo forms of SKD1 exist as
monomers, even though the conformations of the ADP- and ATP-bound forms are
nearly identical. Nucleotide-bound SKD1 structures are compatible with a
hexameric ring arrangement reminiscent of the AAA ATPase p97 D1 ring. In the
hexameric ring model of SKD1, Arg290 from a neighboring molecule binds to the
gamma-phosphate of ATP, which promotes oligomerization of the ATP-bound form.
ATP hydrolysis would eliminate this interaction and subsequent nucleotide
release causes the domains to rotate, which together lead to the disassembly of
the SKD1 oligomer.
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