 |
PDBsum entry 4fxc
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
4fxc
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Tertiary structure of [2fe-2s] ferredoxin from spirulina platensis refined at 2.5 a resolution: structural comparisons of plant-Type ferredoxins and an electrostatic potential analysis.
|
 |
|
Authors
|
 |
K.Fukuyama,
N.Ueki,
H.Nakamura,
T.Tsukihara,
H.Matsubara.
|
 |
|
Ref.
|
 |
J Biochem (tokyo), 1995,
117,
1017-1023.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The structure of plant-type [2Fe-2S] ferredoxin isolated from Spirulina
platensis has been refined using diffraction data to 2.5 A resolution by
alternate cycles of simulated annealing and manual revision of the model. The
final R factor is 19.9% for 2,912 reflections with F > 2 sigma F between 8.0
and 2.5 A resolution. S. platensis ferredoxin, like other plant-type [2Fe-2S]
ferredoxins, has a major alpha-helix flanking a sheet consisting of four beta
strands. The present refinement revises the conformation of residues 56-71, in
which a one-turn helix was identified. Superposition of the Spirulina ferredoxin
structure on the structures of other ferredoxins that have been well refined
showed structural perturbation at a few residues on the amino and carboxyl
termini and the turn between the first and second beta-strands. The
root-mean-square deviations of the corresponding C alpha atoms of the pairs of
ferredoxins range from 0.90 to 1.17 A for all the residues, but from 0.64 to
0.70 A if the few perturbed residues are excluded. Therefore, it may be
concluded that the main-chain foldings of all the plant-type [2Fe-2S]
ferredoxins are essentially the same. Electrostatic potential analysis showed
that the molecular surface around the cluster is negatively charged, whereas
that of the beta-sheet of the other side is positively charged. The interaction
between ferredoxin and ferredoxin-NADP+ reductase is discussed on the basis of
the charge distributions of these molecules and biochemical data.
|
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
X-Ray analysis of a [2fe-2s] ferrodoxin from spirulina platensis. Main chain fold and location of side chains at 2.5 a resolution.
|
 |
|
Authors
|
 |
T.Tsukihira,
K.Fukuyama,
M.Nakamura,
Y.Katsube,
N.Tanaka,
M.Kakudo,
K.Wada,
T.Hase,
H.Matsubara.
|
 |
|
Ref.
|
 |
J Biochem (tokyo), 1981,
90,
1763-1773.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #2
|
 |
|
Title
|
 |
Structure of s. Platensis (2fe-2s) ferredoxin and evolution of chloroplast-Type ferredoxins
|
 |
|
Authors
|
 |
K.Fukuyama,
T.Hase,
S.Matsumoto,
T.Tsukihara,
Y.Katsube,
N.Tanaka,
M.Kakudo,
K.Wada,
H.Matsubara.
|
 |
|
Ref.
|
 |
nature, 1980,
286,
522.
|
 |
 |
|
Secondary reference #3
|
 |
|
Title
|
 |
X-Ray analysis of ferredoxin from spirulina platensis. Ii. Chelate structure of active center.
|
 |
|
Authors
|
 |
T.Tsukihara,
K.Fukuyama,
H.Tahara,
Y.Katsube,
Y.Matsuura,
N.Tanaka,
M.Kakudo,
K.Wada,
H.Matsubara.
|
 |
|
Ref.
|
 |
J Biochem (tokyo), 1978,
84,
1645-1647.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #4
|
 |
|
Title
|
 |
Location of the iron-Sulfur cluster in spirulina platensis ferredoxin by x-Ray analysis
|
 |
|
Authors
|
 |
K.Ogawa,
T.Tsukihara,
H.Tahara,
Y.Katsube,
Y.Matsu-Ura,
N.Tanaka,
M.Kakudo,
K.Wada,
H.Matsubara.
|
 |
|
Ref.
|
 |
atlas of protein sequence, 1978,
5,
54.
|
 |
 |
|
|
|
|
 |