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PDBsum entry 4fxc

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Electron transport PDB id
4fxc
Contents
Protein chain
98 a.a.
Ligands
FES
Waters ×42

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 8586613
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 6801028
Abstract
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 104982
Abstract
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.
PROCHECK
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