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PDBsum entry 3bsd
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Photosynthesis
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PDB id
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3bsd
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Contents |
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* Residue conservation analysis
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Febs Lett
564:274-280
(2004)
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PubMed id:
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Evolution of photosystem I - from symmetry through pseudo-symmetry to asymmetry.
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A.Ben-Shem,
F.Frolow,
N.Nelson.
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ABSTRACT
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The evolution of photosystem (PS) I was probably initiated by the formation of a
homodimeric reaction center similar to the one currently present in green
bacteria. Gene duplication has generated a heterodimeric reaction center that
subsequently evolved to the PSI present in cyanobacteria, algae and plant
chloroplasts. During the evolution of PSI several attempts to maximize the
efficiency of light harvesting took place in the various organisms. In the
Chlorobiaceae, chlorosomes and FMO were added to the homodimeric reaction
center. In cyanobacteria phycobilisomes and CP43' evolved to cope with the light
limitations and stress conditions. The plant PSI utilizes a modular arrangement
of membrane light-harvesting proteins (LHCI). We obtained structural information
from the two ends of the evolutionary spectrum. Novel features in the structure
of Chlorobium tepidum FMO are reported in this communication. Our structure of
plant PSI reveals that the addition of subunit G provided the template for LHCI
binding, and the addition of subunit H prevented the possibility of trimer
formation and provided a binding site for LHCII and the onset of energy
spillover from PSII to PSI.
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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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C.R.Larson,
C.O.Seng,
L.Lauman,
H.J.Matthies,
J.Wen,
R.E.Blankenship,
and
J.P.Allen
(2011).
The three-dimensional structure of the FMO protein from Pelodictyon phaeum and the implications for energy transfer.
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Photosynth Res,
107,
139-150.
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PDB code:
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M.Watanabe,
H.Kubota,
H.Wada,
R.Narikawa,
and
M.Ikeuchi
(2011).
Novel supercomplex organization of photosystem I in Anabaena and Cyanophora paradoxa.
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Plant Cell Physiol,
52,
162-168.
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A.Amunts,
H.Toporik,
A.Borovikova,
and
N.Nelson
(2010).
Structure determination and improved model of plant photosystem I.
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J Biol Chem,
285,
3478-3486.
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PDB codes:
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M.T.Milder,
B.Brüggemann,
R.van Grondelle,
and
J.L.Herek
(2010).
Revisiting the optical properties of the FMO protein.
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Photosynth Res,
104,
257-274.
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M.Ã.˜.Pedersen,
J.Linnanto,
N.U.Frigaard,
N.C.Nielsen,
and
M.Miller
(2010).
A model of the protein-pigment baseplate complex in chlorosomes of photosynthetic green bacteria.
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Photosynth Res,
104,
233-243.
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Y.Tsukatani,
J.Wen,
R.E.Blankenship,
and
D.A.Bryant
(2010).
Characterization of the FMO protein from the aerobic chlorophototroph, Candidatus Chloracidobacterium thermophilum.
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Photosynth Res,
104,
201-209.
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A.Amunts,
and
N.Nelson
(2009).
Plant photosystem I design in the light of evolution.
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Structure,
17,
637-650.
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D.E.Tronrud,
J.Wen,
L.Gay,
and
R.E.Blankenship
(2009).
The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria.
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Photosynth Res,
100,
79-87.
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PDB codes:
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J.Wen,
H.Zhang,
M.L.Gross,
and
R.E.Blankenship
(2009).
Membrane orientation of the FMO antenna protein from Chlorobaculum tepidum as determined by mass spectrometry-based footprinting.
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Proc Natl Acad Sci U S A,
106,
6134-6139.
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L.O.Björn,
G.C.Papageorgiou,
R.E.Blankenship,
and
Govindjee
(2009).
A viewpoint: Why chlorophyll a?
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Photosynth Res,
99,
85-98.
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L.Peng,
H.Shimizu,
and
T.Shikanai
(2008).
The Chloroplast NAD(P)H Dehydrogenase Complex Interacts with Photosystem I in Arabidopsis.
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J Biol Chem,
283,
34873-34879.
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S.Eberhard,
G.Finazzi,
and
F.A.Wollman
(2008).
The dynamics of photosynthesis.
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Annu Rev Genet,
42,
463-515.
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A.Amunts,
O.Drory,
and
N.Nelson
(2007).
The structure of a plant photosystem I supercomplex at 3.4 A resolution.
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Nature,
447,
58-63.
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PDB code:
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C.D.van der Weij-de Wit,
J.A.Ihalainen,
R.van Grondelle,
and
J.P.Dekker
(2007).
Excitation energy transfer in native and unstacked thylakoid membranes studied by low temperature and ultrafast fluorescence spectroscopy.
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Photosynth Res,
93,
173-182.
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J.B.Pereira-Leal,
E.D.Levy,
C.Kamp,
and
S.A.Teichmann
(2007).
Evolution of protein complexes by duplication of homomeric interactions.
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Genome Biol,
8,
R51.
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M.Ã.˜.Pedersen,
J.Borch,
P.Højrup,
R.P.Cox,
and
M.Miller
(2006).
The light-harvesting antenna of Chlorobium tepidum: interactions between the FMO protein and the major chlorosome protein CsmA studied by surface plasmon resonance.
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Photosynth Res,
89,
63-69.
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N.Nelson,
and
C.F.Yocum
(2006).
Structure and function of photosystems I and II.
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Annu Rev Plant Biol,
57,
521-565.
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W.K.Kim,
A.Henschel,
C.Winter,
and
M.Schroeder
(2006).
The many faces of protein-protein interactions: A compendium of interface geometry.
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PLoS Comput Biol,
2,
e124.
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A.Amunts,
A.Ben-Shem,
and
N.Nelson
(2005).
Solving the structure of plant photosystem I--biochemistry is vital.
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Photochem Photobiol Sci,
4,
1011-1015.
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C.Jolley,
A.Ben-Shem,
N.Nelson,
and
P.Fromme
(2005).
Structure of plant photosystem I revealed by theoretical modeling.
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J Biol Chem,
280,
33627-33636.
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PDB code:
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N.Nelson,
and
A.Ben-Shem
(2005).
The structure of photosystem I and evolution of photosynthesis.
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Bioessays,
27,
914-922.
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P.Kiley,
X.Zhao,
M.Vaughn,
M.A.Baldo,
B.D.Bruce,
and
S.Zhang
(2005).
Self-assembling peptide detergents stabilize isolated photosystem I on a dry surface for an extended time.
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PLoS Biol,
3,
e230.
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R.Kouril,
N.van Oosterwijk,
A.E.Yakushevska,
and
E.J.Boekema
(2005).
Photosystem I: a search for green plant trimers.
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Photochem Photobiol Sci,
4,
1091-1094.
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T.Morosinotto,
M.Ballottari,
F.Klimmek,
S.Jansson,
and
R.Bassi
(2005).
The association of the antenna system to photosystem I in higher plants. Cooperative interactions stabilize the supramolecular complex and enhance red-shifted spectral forms.
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J Biol Chem,
280,
31050-31058.
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N.Nelson,
and
A.Ben-Shem
(2004).
The complex architecture of oxygenic photosynthesis.
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Nat Rev Mol Cell Biol,
5,
971-982.
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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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