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PDBsum entry 1t1c
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Photoreceptor
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PDB id
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1t1c
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Contents |
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* Residue conservation analysis
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DOI no:
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Structure
13:55-63
(2005)
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PubMed id:
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A structural pathway for signaling in the E46Q mutant of photoactive yellow protein.
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S.Rajagopal,
S.Anderson,
V.Srajer,
M.Schmidt,
R.Pahl,
K.Moffat.
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ABSTRACT
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In the bacterial photoreceptor photoactive yellow protein (PYP), absorption of
blue light by its chromophore leads to a conformational change in the protein
associated with differential signaling activity, as it executes a reversible
photocycle. Time-resolved Laue crystallography allows structural snapshots (as
short as 150 ps) of high crystallographic resolution (approximately 1.6 A) to be
taken of a protein as it functions. Here, we analyze by singular value
decomposition a comprehensive time-resolved crystallographic data set of the
E46Q mutant of PYP throughout the photocycle spanning 10 ns-100 ms. We identify
and refine the structures of five distinct intermediates and provide a plausible
chemical kinetic mechanism for their inter conversion. A clear structural
progression is visible in these intermediates, in which a signal generated at
the chromophore propagates through a distinct structural pathway of conserved
residues and results in structural changes near the N terminus, over 20 A
distant from the chromophore.
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Selected figure(s)
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Figure 5.
Figure 5. The Chemical Kinetic Mechanism of E46Q PYP in the
Crystal (A) Chemical kinetic mechanism of E46Q PYP in the
crystal, with rate coefficients (s -1) of 3.0 × 10^6 (IE1->IE2),
5.0 × 10^5 (IE2->IL1), 5.0 × 10^3 (IL1->IL2), 3.0 × 10^3
(IL1->G), 50 (IL2->IL3), and 0 (IL3->G). (B) Predicted
concentrations of IE1 (red), IE2 (magenta), IL1 (blue), IL2
(cyan), IL3 (dashed), and the ground state (black) with the
mechanism in (A). (C) Predicted concentration profiles for
spectroscopic intermediates pR (IE1 and IE2) shown in red, pB
(IL1 and IL2) shown in blue, and the ground state (IL3 and pG)
shown in black with the mechanism in (A).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2005,
13,
55-63)
copyright 2005.
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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Schmidt,
T.Graber,
R.Henning,
and
V.Srajer
(2010).
Five-dimensional crystallography.
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Acta Crystallogr A,
66,
198-206.
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S.Westenhoff,
E.Nazarenko,
E.Malmerberg,
J.Davidsson,
G.Katona,
and
R.Neutze
(2010).
Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches.
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Acta Crystallogr A,
66,
207-219.
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A.Möglich,
R.A.Ayers,
and
K.Moffat
(2009).
Structure and signaling mechanism of Per-ARNT-Sim domains.
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Structure,
17,
1282-1294.
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A.Specht,
F.Bolze,
Z.Omran,
J.F.Nicoud,
and
M.Goeldner
(2009).
Photochemical tools to study dynamic biological processes.
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HFSP J,
3,
255-264.
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D.Hoersch,
H.Otto,
M.A.Cusanovich,
and
M.P.Heyn
(2009).
Time-resolved spectroscopy of dye-labeled photoactive yellow protein suggests a pathway of light-induced structural changes in the N-terminal cap.
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Phys Chem Chem Phys,
11,
5437-5444.
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P.A.Sigala,
M.A.Tsuchida,
and
D.Herschlag
(2009).
Hydrogen bond dynamics in the active site of photoactive yellow protein.
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Proc Natl Acad Sci U S A,
106,
9232-9237.
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J.Vreede,
K.J.Hellingwerf,
and
P.G.Bolhuis
(2008).
Helix formation is a dynamical bottleneck in the recovery reaction of Photoactive Yellow Protein.
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Proteins,
72,
136-149.
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M.A.van der Horst,
J.C.Arents,
R.Kort,
and
K.J.Hellingwerf
(2007).
Binding, tuning and mechanical function of the 4-hydroxy-cinnamic acid chromophore in photoactive yellow protein.
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Photochem Photobiol Sci,
6,
571-579.
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S.Z.Fisher,
S.Anderson,
R.Henning,
K.Moffat,
P.Langan,
P.Thiyagarajan,
and
A.J.Schultz
(2007).
Neutron and X-ray structural studies of short hydrogen bonds in photoactive yellow protein (PYP).
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Acta Crystallogr D Biol Crystallogr,
63,
1178-1184.
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PDB code:
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T.De la Mora-Rey,
and
C.M.Wilmot
(2007).
Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography.
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Curr Opin Struct Biol,
17,
580-586.
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B.Borucki,
C.P.Joshi,
H.Otto,
M.A.Cusanovich,
and
M.P.Heyn
(2006).
The transient accumulation of the signaling state of photoactive yellow protein is controlled by the external pH.
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Biophys J,
91,
2991-3001.
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N.Shimizu,
Y.Imamoto,
M.Harigai,
H.Kamikubo,
Y.Yamazaki,
and
M.Kataoka
(2006).
pH-dependent equilibrium between long lived near-UV intermediates of photoactive yellow protein.
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J Biol Chem,
281,
4318-4325.
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R.Brudler,
C.R.Gessner,
S.Li,
S.Tyndall,
E.D.Getzoff,
and
V.L.Woods
(2006).
PAS domain allostery and light-induced conformational changes in photoactive yellow protein upon I2 intermediate formation, probed with enhanced hydrogen/deuterium exchange mass spectrometry.
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J Mol Biol,
363,
148-160.
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S.Yeremenko,
I.H.van Stokkum,
K.Moffat,
and
K.J.Hellingwerf
(2006).
Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy.
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Biophys J,
90,
4224-4235.
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D.Bourgeois,
and
A.Royant
(2005).
Advances in kinetic protein crystallography.
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Curr Opin Struct Biol,
15,
538-547.
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J.Vreede,
W.Crielaard,
K.J.Hellingwerf,
and
P.G.Bolhuis
(2005).
Predicting the signaling state of photoactive yellow protein.
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Biophys J,
88,
3525-3535.
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S.Yeremenko,
and
K.J.Hellingwerf
(2005).
Resolving protein structure dynamically.
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Structure,
13,
4-6.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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}
}
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