 |
PDBsum entry 2pps
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Photosynthesis
|
PDB id
|
|
|
|
2pps
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
478 a.a.*
|
|
|
|
|
|
|
|
|
|
|
503 a.a.*
|
|
|
|
|
|
|
|
|
|
|
111 a.a.*
|
|
|
|
|
|
|
|
|
|
|
64 a.a.*
|
|
|
|
|
|
|
|
|
|
|
130 a.a.*
|
|
|
|
|
|
|
|
|
|
|
80 a.a.*
|
|
|
|
|
|
|
|
|
* C-alpha coords only
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Photosystem I at 4 a resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system.
|
|
|
Authors
|
|
N.Krauss,
W.D.Schubert,
O.Klukas,
P.Fromme,
H.T.Witt,
W.Saenger.
|
|
|
Ref.
|
|
Nat Struct Biol, 1996,
3,
965-973.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The 4 A X-ray structure model of trimeric photosystem I of the cyanobacterium
Synechococcus elongatus reveals 31 transmembrane, nine surface and three stromal
alpha-helices per monomer, assigned to the 11 protein subunits: PsaA and PsaB
are related by a pseudo two-fold axis normal to the membrane plane, along which
the electron transfer pigments are arranged. 65 antenna chlorophyll a (Chl a)
molecules separated by < or = 16 A form an oval, clustered net continuous
with the electron transfer chain through the second and third Chl a pairs of the
electron transfer system. This suggests a dual role for these Chl a both in
excitation energy and electron transfer. The architecture of the protein core
indicates quinone and iron-sulphur type reaction centres to have a common
ancestor.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Photosystem I of synechococcus elongatus at 4 a resolution: comprehensive structure analysis.
|
|
|
Authors
|
|
W.D.Schubert,
O.Klukas,
N.Krauss,
W.Saenger,
P.Fromme,
H.T.Witt.
|
|
|
Ref.
|
|
J Mol Biol, 1997,
272,
741-769.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 4.
Figure 4. (a) View from the stromal side. The PSI trimer is
approximately discoidal, monomers being separated by lateral
indentations. The maximal distance from the C[3] axis to the
peripheral surface is  vert,
similar 105 (±5) Å. Membrane-integral subunits are
indicated in white; the subunits of the stromal ridge are
indicated in colour: PsaC, yellow, PsaD, red; PsaE, blue. The
binding pocket for ferredoxin/flavodoxin, formed by PsaC, PsaD,
PsaE and a-helix e' of either PsaA or PsaB, on the side of the
ridge distal from the C[3]-axis is indicated; asterisk: crystal
contact. (b) View along the membrane plane, i.e. view as in (a)
but flipped about the horizontal through 90°. (Produced
using Grasp; [Nicholls et al 1991].)
|
|
Figure 9.
Figure 9. (a) Stereographic view of all 86 Chla molecules
presently identified, seen from the stromal side. Chla are
modelled as porphyrin structures, indicating their positions and
planar orientations. The region occupied by the core antenna
system largely lies within an elliptical, open-cylindrical
region. It is located between the inner reaction centre and the
outer delimiting ring of α-helices composed of the N-terminal
of the large subunits PsaA and PsaB and those of the smaller
membrane integral subunits PsaI, PsaL, PsaM, PsaJ and PsaF (see
shaded region in Figure 5). The Chla of the electron transfer
system are coloured red and connecting Chla light blue. Pink
Chla are conspicuously oriented and arranged as closely spaced
Chla pairs. (b) An analytical description of the antenna system
Chla distribution plotting the inclination (relative to the
membrane normal) of each porphyrin plane against its relative
membrane depth. The membrane-integral region is divided into a
lumenal (bottom), a middle and a stromal third, while porphyrin
plane inclinations are grouped into the categories strongly (0
to 30°, left), moderately (30 to 60°, central) and
weakly aligned (60 to 90°, right) with the membrane normal.
The number of Chla in each region (including Image but excluding
all eC) is indicated near the right-hand side of the field,
horizontal and vertical summations being indicated on the
right-hand side and at the top of the Figure (further discussion
see the text.).
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from Elsevier
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Present state of the crystal structure analysis of photosystem i at 4.5 a resolution
|
|
|
Authors
|
|
W.D.Schubert,
O.Klukas,
N.Krauss,
W.Saenger,
P.Fromme,
H.T.Witt.
|
|
|
Ref.
|
|
photosynthesis : from light, 1995,
2,
3.
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Three-Dimensional structure of system i of photosynthesis at 6a resolution,
|
|
|
Authors
|
|
N.Krauss,
W.Hinrichs,
I.Witt,
P.Fromme,
W.Pritzkow,
Z.Dauter,
C.Betzel,
K.S.Wilson,
H.T.Witt,
W.Saenger.
|
|
|
Ref.
|
|
nature, 1993,
361,
326.
|
|
|
|
Secondary reference #4
|
|
|
Title
|
|
X-Ray characterization of single crystals of the reaction center i of water splitting photosynthesis
|
|
|
Authors
|
|
I.Witt,
H.T.Witt,
D.Di fiore,
M.Rogner,
W.Hinrichs,
W.Saenger,
J.Granzin,
C.Betzel,
Z.Dauter.
|
|
|
Ref.
|
|
ber bunsenges phys chem, 1988,
92,
1503.
|
|
|
|
|
|
|
|
|
Headers
|
|
|
|
|
|
