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332 a.a.
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273 a.a.
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323 a.a.
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258 a.a.
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* Residue conservation analysis
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PDB id:
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Photosynthesis
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Title:
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Photosynthetic reaction center blastochloris viridis (atcc)
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Structure:
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Photosynthetic reaction center cytochromE C subunit precursor. Chain: c. Synonym: c558/c559. Reaction center protein l chain. Chain: l. Synonym: photosynthetic reaction center l subunit. Reaction center protein m chain. Chain: m.
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Source:
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Blastochloris viridis. Organism_taxid: 1079. Organism_taxid: 1079
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Biol. unit:
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Tetramer (from
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Resolution:
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2.86Å
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R-factor:
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0.202
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R-free:
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0.228
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Authors:
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R.H.Baxter,N.Ponomarenko,R.Pahl,V.Srajer,K.Moffat,J.R.Norris
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Key ref:
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R.H.Baxter
et al.
(2004).
Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center.
Proc Natl Acad Sci U S A,
101,
5982-5987.
PubMed id:
DOI:
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Date:
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26-Sep-03
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Release date:
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27-Apr-04
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PROCHECK
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Headers
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References
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P07173
(CYCR_BLAVI) -
Photosynthetic reaction center cytochrome c subunit from Blastochloris viridis
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Seq: Struc:
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356 a.a.
332 a.a.
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P06009
(RCEL_BLAVI) -
Reaction center protein L chain from Blastochloris viridis
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Seq: Struc:
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274 a.a.
273 a.a.
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DOI no:
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Proc Natl Acad Sci U S A
101:5982-5987
(2004)
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PubMed id:
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Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center.
|
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R.H.Baxter,
N.Ponomarenko,
V.Srajer,
R.Pahl,
K.Moffat,
J.R.Norris.
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ABSTRACT
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Light-induced structural changes in the bacterial reaction center were studied
by a time-resolved crystallographic experiment. Crystals of protein from
Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted
with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark
and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse,
7 ns duration). Refinement of monochromatic data shows that ubiquinone binds
only in the "proximal" Q(B) binding site. No significant structural
difference was observed between the light and dark datasets; in particular, no
quinone motion was detected. This result may be reconciled with previous studies
by postulating equilibration of the "distal" and "proximal"
binding sites upon extended dark adaption, and in which movement of ubiquinone
is not the conformational gate for the first electron transfer between Q(A) and
Q(B).
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Selected figure(s)
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Figure 1.
Fig. 1. The Q[B] binding site and its immediate
environment, showing the two positions observed for ubiquinone
binding. The distal position is shown in purple, the proximal in
orange. Shown are coordinates from 1AIG [PDB]
and 1AIJ [PDB]
(16). Figs. 1, 3 and 4 were prepared with PYMOL.
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Figure 3.
Fig. 3. Electron density for the Q[B] binding pocket. 2F[o]
- F[c] maps show density from a simulated-annealing omit map
omitting Q[B] (green) and density for the refined model (cyan).
(A) Monochromatic dataset, 2.9-Å resolution, contour level
0.5 .(B) Dark Laue dataset,
3.3-Å resolution, contoured at 0.3 .
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Figures were
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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|
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A.B.Wöhri,
G.Katona,
L.C.Johansson,
E.Fritz,
E.Malmerberg,
M.Andersson,
J.Vincent,
M.Eklund,
M.Cammarata,
M.Wulff,
J.Davidsson,
G.Groenhof,
and
R.Neutze
(2010).
Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction.
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Science,
328,
630-633.
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PDB codes:
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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.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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H.Ohmori,
L.Nagy,
M.Dorogi,
and
M.Terazima
(2008).
Charge stabilization in reaction center protein investigated by optical heterodyne detected transient grating spectroscopy.
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Eur Biophys J,
37,
1167-1174.
|
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J.Pieper,
T.Hauss,
A.Buchsteiner,
and
G.Renger
(2008).
The effect of hydration on protein flexibility in photosystem II of green plants studied by quasielastic neutron scattering.
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Eur Biophys J,
37,
657-663.
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D.Bourgeois,
F.Schotte,
M.Brunori,
and
B.Vallone
(2007).
Time-resolved methods in biophysics. 6. Time-resolved Laue crystallography as a tool to investigate photo-activated protein dynamics.
|
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Photochem Photobiol Sci,
6,
1047-1056.
|
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L.Li,
D.Mustafi,
Q.Fu,
V.Tereshko,
D.L.Chen,
J.D.Tice,
and
R.F.Ismagilov
(2006).
Nanoliter microfluidic hybrid method for simultaneous screening and optimization validated with crystallization of membrane proteins.
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Proc Natl Acad Sci U S A,
103,
19243-19248.
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PDB code:
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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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|
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|
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H.Ihee,
S.Rajagopal,
V.Srajer,
R.Pahl,
S.Anderson,
M.Schmidt,
F.Schotte,
P.A.Anfinrud,
M.Wulff,
and
K.Moffat
(2005).
Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds.
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| |
Proc Natl Acad Sci U S A,
102,
7145-7150.
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PDB codes:
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H.Ishikita,
and
E.W.Knapp
(2005).
Induced conformational changes upon Cd2+ binding at photosynthetic reaction centers.
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Proc Natl Acad Sci U S A,
102,
16215-16220.
|
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L.Giachini,
F.Francia,
A.Mallardi,
G.Palazzo,
E.Carpenè,
F.Boscherini,
and
G.Venturoli
(2005).
Multiple scattering x-ray absorption studies of Zn2+ binding sites in bacterial photosynthetic reaction centers.
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Biophys J,
88,
2038-2046.
|
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|
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|
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R.H.Baxter,
B.L.Seagle,
N.Ponomarenko,
and
J.R.Norris
(2005).
Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark.
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Acta Crystallogr D Biol Crystallogr,
61,
605-612.
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PDB code:
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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
codes are
shown on the right.
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');
}
}
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