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PDBsum entry 2wsf
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Photosynthesis
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PDB id
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2wsf
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Contents |
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165 a.a.
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176 a.a.
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153 a.a.
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166 a.a.
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730 a.a.
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733 a.a.
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81 a.a.
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138 a.a.
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65 a.a.
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154 a.a.
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95 a.a.
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69 a.a.
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30 a.a.
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42 a.a.
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84 a.a.
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162 a.a.
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85 a.a.
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53 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure determination and improved model of plant photosystem i.
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Authors
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A.Amunts,
H.Toporik,
A.Borovikova,
N.Nelson.
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Ref.
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J Biol Chem, 2010,
285,
3478-3486.
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PubMed id
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Abstract
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Photosystem I functions as a sunlight energy converter, catalyzing one of the
initial steps in driving oxygenic photosynthesis in cyanobacteria, algae, and
higher plants. Functionally, Photosystem I captures sunlight and transfers the
excitation energy through an intricate and precisely organized antenna system,
consisting of a pigment network, to the center of the molecule, where it is used
in the transmembrane electron transfer reaction. Our current understanding of
the sophisticated mechanisms underlying these processes has profited greatly
from elucidation of the crystal structures of the Photosystem I complex. In this
report, we describe the developments that ultimately led to enhanced structural
information of plant Photosystem I. In addition, we report an improved
crystallographic model at 3.3-A resolution, which allows analysis of the
structure in more detail. An improved electron density map yielded
identification and tracing of subunit PsaK. The location of an additional ten
beta-carotenes as well as five chlorophylls and several loop regions, which were
previously uninterpretable, are now modeled. This represents the most complete
plant Photosystem I structure obtained thus far, revealing the locations of and
interactions among 17 protein subunits and 193 non-covalently bound
photochemical cofactors. Using the new crystal structure, we examine the network
of contacts among the protein subunits from the structural perspective, which
provide the basis for elucidating the functional organization of the complex.
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