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PDBsum entry 5h2f
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Photosynthesis
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PDB id
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5h2f
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334 a.a.
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505 a.a.
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451 a.a.
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342 a.a.
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79 a.a.
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33 a.a.
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63 a.a.
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35 a.a.
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36 a.a.
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37 a.a.
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35 a.a.
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243 a.a.
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30 a.a.
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97 a.a.
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137 a.a.
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29 a.a.
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37 a.a.
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62 a.a.
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31 a.a.
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36 a.a.
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40 a.a.
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36 a.a.
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×2
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×70
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×4
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×18
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×12
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×4
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×12
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×8
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×11
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×27
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×2
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×2
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×2
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PDB id:
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| Name: |
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Photosynthesis
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Title:
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Crystal structure of the psbm-deletion mutant of photosystem ii
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Structure:
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Photosystem ii protein d1 1. Chain: a, a. Fragment: unp residues 11-344. Synonym: psii d1 protein 1,photosystem ii q(b) protein 1. Photosystem ii cp47 reaction center protein. Chain: b, b. Fragment: unp residues 2-506. Synonym: psii 47 kda protein,protein cp-47. Photosystem ii cp43 reaction center protein.
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Source:
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Thermosynechococcus elongatus (strain bp-1). Organism_taxid: 197221. Strain: bp-1. Thermosynechococcus elongatus. Strain: bp-1
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Resolution:
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2.20Å
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R-factor:
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0.177
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R-free:
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0.226
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Authors:
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S.Uto,K.Kawakami,Y.Umena,M.Iwai,M.Ikeuchi,J.R.Shen,N.Kamiya
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Key ref:
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S.Uto
et al.
(2017).
Mutual relationships between structural and functional changes in a PsbM-deletion mutant of photosystem II.
Faraday Discuss,
198,
107-120.
PubMed id:
DOI:
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Date:
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15-Oct-16
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Release date:
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22-Mar-17
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PROCHECK
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Headers
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References
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P0A444
(PSBA1_THEEB) -
Photosystem II protein D1 1 from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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360 a.a.
334 a.a.
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Q8DIQ1
(PSBB_THEEB) -
Photosystem II CP47 reaction center protein from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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510 a.a.
505 a.a.
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Q8DIF8
(PSBC_THEEB) -
Photosystem II CP43 reaction center protein from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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461 a.a.
451 a.a.
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Q8CM25
(PSBD_THEEB) -
Photosystem II D2 protein from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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352 a.a.
342 a.a.
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Q8DIP0
(PSBE_THEEB) -
Cytochrome b559 subunit alpha from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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84 a.a.
79 a.a.
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Q8DIN9
(PSBF_THEEB) -
Cytochrome b559 subunit beta from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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45 a.a.
33 a.a.
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Q8DJ43
(PSBH_THEEB) -
Photosystem II reaction center protein H from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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66 a.a.
63 a.a.
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Q8DJZ6
(PSBI_THEEB) -
Photosystem II reaction center protein I from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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38 a.a.
35 a.a.*
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P59087
(PSBJ_THEEB) -
Photosystem II reaction center protein J from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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40 a.a.
36 a.a.
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Q9F1K9
(PSBK_THEEB) -
Photosystem II reaction center protein K from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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46 a.a.
37 a.a.
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Q8DIN8
(PSBL_THEEB) -
Photosystem II reaction center protein L from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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37 a.a.
35 a.a.
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P0A431
(PSBO_THEEB) -
Photosystem II extrinsic protein O from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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272 a.a.
243 a.a.
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Q8DIQ0
(PSBT_THEEB) -
Photosystem II reaction center protein T from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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32 a.a.
30 a.a.*
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Q9F1L5
(PSBU_THEEB) -
Photosystem II extrinsic protein U from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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134 a.a.
97 a.a.
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P0A386
(CY550_THEEB) -
Photosystem II extrinsic protein V from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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163 a.a.
137 a.a.
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Q8DJI1
(YCF12_THEEB) -
Photosystem II reaction center protein Psb30 from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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46 a.a.
29 a.a.
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Q9F1R6
(PSBX_THEEB) -
Photosystem II reaction center protein X from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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41 a.a.
37 a.a.
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Q8DHJ2
(PSBZ_THEEB) -
Photosystem II reaction center protein Z from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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62 a.a.
62 a.a.
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Q8DIN9
(PSBF_THEEB) -
Cytochrome b559 subunit beta from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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45 a.a.
31 a.a.
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Q8DJZ6
(PSBI_THEEB) -
Photosystem II reaction center protein I from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
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Seq: Struc:
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38 a.a.
36 a.a.*
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Enzyme class:
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Chains A, D, a, d:
E.C.1.10.3.9
- photosystem Ii.
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Reaction:
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2 a plastoquinone + 4 hnu + 2 H2O = 2 a plastoquinol + O2
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2
×
a plastoquinone
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+
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4
×
hnu
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+
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2
×
H2O
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=
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2
×
a plastoquinol
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+
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O2
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Faraday Discuss
198:107-120
(2017)
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PubMed id:
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Mutual relationships between structural and functional changes in a PsbM-deletion mutant of photosystem II.
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S.Uto,
K.Kawakami,
Y.Umena,
M.Iwai,
M.Ikeuchi,
J.R.Shen,
N.Kamiya.
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ABSTRACT
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Photosystem II (PSII) is a membrane protein complex that performs light-induced
electron transfer and oxygen evolution from water. PSII consists of 19 or 20
subunits in its crystal form and binds various cofactors such as chlorophyll a,
plastoquinone, carotenoid, and lipids. After initial light excitation, the
charge separation produces an electron, which is transferred to a plastoquinone
molecule (QA) and then to another plastoquinone (QB). PsbM
is a low-molecular-weight subunit with one transmembrane helix, and is located
in the monomer-monomer interface of the PSII dimer. The function of PsbM has
been reported to be stabilization of the PSII dimer and maintenance of electron
transfer efficiency of PSII based on previous X-ray crystal structure analysis
at a resolution of 4.2 Å. In order to elucidate the structure-function
relationships of PsbM in detail, we improved the quality of PSII crystals from a
PsbM-deleted mutant (ΔPsbM-PSII) of Thermosynechococcus elongatus, and
succeeded in improving the diffraction quality to a resolution of 2.2 Å. X-ray
crystal structure analysis of ΔPsbM-PSII showed that electron densities for the
PsbM subunit and neighboring carotenoid and detergent molecules were absent in
the monomer-monomer interface. The overall structure of ΔPsbM-PSII was similar
to wild-type PSII, but the arrangement of the hydrophobic transmembrane subunits
was significantly changed by the deletion of PsbM, resulting in a slight
widening of the lipid hole involving QB. The lipid hole-widening
further induced structural changes of the bicarbonate ion coordinated to the
non-heme Fe(ii) atom and destabilized the polypeptide chains around the
QBbinding site located far from the position of PsbM. The
fluorescence decay measurement indicated that the electron transfer rate from
QAto QBwas decreased in ΔPsbM-PSII compared with
wild-type PSII. The functional change in electron transfer efficiency was fully
interpreted based on structural changes caused by the deletion of the PsbM
subunit.
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');
}
}
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