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PDBsum entry 1v2b
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Photosynthesis
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PDB id
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1v2b
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the psbp protein of photosystem ii from nicotiana tabacum.
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Authors
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K.Ifuku,
T.Nakatsu,
H.Kato,
F.Sato.
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Ref.
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EMBO Rep, 2004,
5,
362-367.
[DOI no: ]
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PubMed id
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Abstract
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PsbP is a membrane-extrinsic subunit of the water-oxidizing complex photosystem
II (PS II). The evolutionary origin of PsbP has long been a mystery because it
specifically exists in higher plants and green algae but not in cyanobacteria.
We report here the crystal structure of PsbP from Nicotiana tabacum at a
resolution of 1.6 A. Its structure is mainly composed of beta-sheet, and is not
similar to any structures in cyanobacterial PS II. However, the electrostatic
surface potential of PsbP is similar to that of cyanobacterial PsbV (cyt
c(550)), which has a function similar to PsbP. A structural homology search with
the DALI algorithm indicated that the folding of PsbP is very similar to that of
Mog1p, a regulatory protein for the nuclear transport of Ran GTPase. The
structure of PsbP provides insight into its novel function in GTP-regulated
metabolism in PS II.
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Figure 2.
Figure 2 Stereo view of the structure of PsbP. The schematic
representation of the PsbP structural model shows a series of
 -strands
that are derived from residues 16 -53 (domain I: pink) and the
central six-stranded antiparallel -sheet
flanked on both sides by helices (domain II: blue). The N
(residue 16) and C (residue 186) termini are labelled. The
position of the Asn 58 -Val 59 bond is indicated by an arrow.
The figure was generated with PyMOL (http://www.pymol.org).
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Figure 3.
Figure 3 Comparison of the electrostatic surface potentials of
(A) PsbP from N. tabacum (this study) and (B) PsbV from
Thermosynechococcus elongatus (Kerfeld et al, 2003). The
molecules are rotated anticlockwise by 90° and 180° around a
vertical axis (left to right). The figure was produced using
GRASP (Nicholls et al, 1991).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO Rep
(2004,
5,
362-367)
copyright 2004.
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Secondary reference #1
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Title
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Crystallization and preliminary crystallographic studies on the extrinsic 23 kda protein in the oxygen-Evolving complex of photosystem ii.
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Authors
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K.Ifuku,
T.Nakatsu,
H.Kato,
F.Sato.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2003,
59,
1462-1463.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 A typical crystal of OEC23 from Nicotiana tabacum. The
dimensions of the crystal are approximately 0.4 × 0.8 × 0.2 mm.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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A truncated mutant of the extrinsic 23-Kda protein that absolutely requires the extrinsic 17-Kda protein for ca2+ retention in photosystem ii.
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Authors
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K.Ifuku,
F.Sato.
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Ref.
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Plant Cell Physiol, 2002,
43,
1244-1249.
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PubMed id
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Secondary reference #3
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Title
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Importance of the n-Terminal sequence of the extrinsic 23 kda polypeptide in photosystem ii in ion retention in oxygen evolution.
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Authors
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K.Ifuku,
F.Sato.
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Ref.
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Biochim Biophys Acta, 2001,
1546,
196-204.
[DOI no: ]
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PubMed id
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