 |
PDBsum entry 1pcs
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
1pcs
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The 2.15 a crystal structure of a triple mutant plastocyanin from the cyanobacterium synechocystis sp. Pcc 6803.
|
|
|
Authors
|
|
A.Romero,
B.De la cerda,
P.F.Varela,
J.A.Navarro,
M.Hervás,
M.A.De la rosa.
|
|
|
Ref.
|
|
J Mol Biol, 1998,
275,
327-336.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
96%.
|
|
|
|
Abstract
|
|
|
The crystal structure of the triple mutant A42D/D47P/A63L plastocyanin from the
cyanobacterium Synechocystis sp. PCC 6803 has been determined by Patterson
search methods using the known structure of the poplar protein. Crystals of the
triple mutant A42D/D47P/A63L, which are stable for days in its oxidized form,
were grown from ammonium sulfate, with the cell constants a = b = 34.3 A and c =
111.8 A belonging to space group P3(2)21. The structure was refined using
restrained crystallographic refinement to an R-factor of 16.7% for 4070
independent reflections between 8.0 and 2.15 A with intensities greater than 2
sigma (I), with root mean square deviations of 0.013 A and 1.63 degrees from
ideal bond lengths and bond angles, respectively. The final model comprises 727
non-hydrogen protein atoms within 98 residues, 75 water molecules and a single
copper ion. The overall tertiary fold of Synechocystis plastocyanin consists of
a compact ellipsoidal beta-sandwich structure made up of two beta-sheets
embracing a hydrophobic core. Each sheet contains parallel and antiparallel
beta-strands. In addition to the beta-sheets, the structure contains an
alpha-helix from Pro47 to Lys54 that follows beta-strand 4. The
three-dimensional structure of Synechocystis plastocyanin is thus similar to
those reported for the copper protein isolated from eukaryotic organisms and, in
particular, from the cyanobacterium Anabaena variabilis, the only cyanobacterial
plastocyanin structure available so far. The molecule holds an hydrophobic
region surrounding His87, as do other plastocyanins, but the lack of negatively
charged residues at the putative distant remote site surrounding Tyr83 could
explain why the Synechocystis protein exhibits a collisional reaction mechanism
for electron transfer to photosystem I (PSI), which involves no formation of the
transient plastocyanin-PSI complex kinetically observed in green algae and
higher plants.
|
|
|
|
|
|
|
|
Figure 3.
Figure 3. Stereo diagram of the final 2 F[o] − F[c] map,
contoured at 1.0 σ, showing the copper binding site of
Synechocystis mutant plastocyanin. The copper site primarily has
N2S2 coordination and is ligated in a T1 distorted tetrahedral
geometry by His37, His87, Cys84 and Met92.
|
|
Figure 5.
Figure 5. Electrostatic potential mapping at the molecular
surface of plastocyanin from Synechocystis, poplar , C.
reinhardtii and E. prolifera as viewed in the relatively same
orientation. The protein molecule is depicted by a solid
surface, colored according to the calculated electrostatic
potential and contoured from −8 (intense red) to +8kT/e
(intense blue). The Figure was made with GRASP (Nicholls et al.,
1993).
|
|
|
|
|
|
The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1998,
275,
327-336)
copyright 1998.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Solution structure of reduced plastocyanin from the blue-Green alga anabaena variabilis.
|
|
|
Authors
|
|
U.Badsberg,
A.M.Jørgensen,
H.Gesmar,
J.J.Led,
J.M.Hammerstad,
L.L.Jespersen,
J.Ulstrup.
|
|
|
Ref.
|
|
Biochemistry, 1996,
35,
7021-7031.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Structure of oxidized poplar plastocyanin at 1.6 a resolution.
|
|
|
Authors
|
|
J.M.Guss,
H.C.Freeman.
|
|
|
Ref.
|
|
J Mol Biol, 1983,
169,
521-563.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 7.
Fro. 7. Stereo view of the Cu site in Cu-plastocyanin. All on-hydrogen atoms of each ligand residue
(N, C~. C, O, side-chain) are shown.
|
|
Figure 13.
Fro. 13. The same stereo view of the plastocyanin molecule as in Fig. II, but emphasizing acidic
residues that are invariant or conservatively substituted in plant lstocyanins. Residues shown with
black side-chains are Glu25, Asp42, Glu43, Asp44, Set45 (Glu n most other plastoeyanins), AspS1,
Glu59, Asp61 and Glu68. In ddition, Tyr83 nd Gin88 (which are invariant in plant plastocyanins)
am included but not dluwn in lack.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from Elsevier
|
|
|
|
|
|
|
