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PDBsum entry 2x9h
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Contractile protein
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PDB id
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2x9h
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References listed in PDB file
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Key reference
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Title
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Crystal structure of myosin-2 motor domain in complex ADP-Metavanadate and pentachlorocarbazole
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Authors
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R.Fedrov,
M.Boehl,
G.Tsiavaliaris,
F.K.Hartmann,
P.Baruchb.Brenner,
R.Martin,
H.J.Knoelker,
H.O.Gutzeit,
D.J.Manst.
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Ref.
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TO BE PUBLISHED ...
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Secondary reference #1
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Title
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The mechanism of pentabromopseudilin inhibition of myosin motor activity.
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Authors
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R.Fedorov,
M.Böhl,
G.Tsiavaliaris,
F.K.Hartmann,
M.H.Taft,
P.Baruch,
B.Brenner,
R.Martin,
H.J.Knölker,
H.O.Gutzeit,
D.J.Manstein.
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Ref.
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Nat Struct Biol, 2009,
16,
80-88.
[DOI no: ]
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PubMed id
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Figure 1.
(a) Effect of PBP on the steady-state actin-activated ATPase
activitiy of Dd myosin-5b. Actin-activated ATPase activities in
the absence (  square
) and presence of 25  M
PBP (  down
triangle ) are shown. (b) Concentration-dependence of the
inhibition of the actin-activated ATPase activity of different
myosin isoforms in the presence of 0–150 M
PBP. The semilogarithmic plot shows the concentration dependence
for myosin-1E (o), myosin-2 ( square
), Dd myosin-5b (  )
and chicken myosin-5a ( down
triangle ). The concentrations of PBP required for half-maximal
inhibition (IC[50]) of the different myosin motors were
determined from sigmoidal fits of the data. All parameters are
summarized in Table 1. (c) Fluorescence transients obtained upon
mixing 1 M
Dd myosin-5b with 10 M
mantATP in the absence and presence of 5 M,
25 M,
50 M
and 100 M
PBP. The concentration dependence of the amplitude of the fast
phase is shown in the inset. (d) Rate constants for ATP binding
and hydrolysis were determined by following the time-dependent
changes in the intrinsic protein fluorescence of Dd myosin-5b.
Addition of 25 M
PBP leads to a 14-fold reduction in the apparent second-order
rate constant for ATP binding and a ten-fold reduction of the
rate of ATP hydrolysis (Supplementary Methods online). (e)
PBP-mediated inhibition of chicken myosin-5a in the in vitro
motility assay. The histograms show the average sliding velocity
of rhodamine-phalloidin–labeled actin filaments in the absence
and presence of 10 M
PBP.
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Figure 3.
Myosin residues interacting with PBP are shown as predicted
by molecular modeling for Dd myosin-1E (a), Sc Myo2 (b), Gg
myosin-5a (c) and Dd myosin-5b (d).
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The above figures are
reproduced from the cited reference
with permission from Macmillan Publishers Ltd
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