Structure of Synechococcus elongatus [Fe2S2] Ferredoxin in Solution

Baumann, Bettina; Sticht, Heinrich; Schärpf, Manuela; Sutter, M.; Haehnel, Wolfgang; Rösch, Paul

doi:10.1021/bi961144m

Cited by 45 publications

(53 citation statements)

References 46 publications

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“…elongatus ferredoxin After preparation of the manuscript, a structure of the same ferredoxin in solution was published (Baumann et al, 1996). Signi®cant differences exist between the two structures.…”

Section: Natural Strategies Of Ferredoxins For Thermostabilitymentioning

confidence: 99%

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Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Hatanaka

Tanimura

Katoh

et al. 1997

Journal of Molecular Biology

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Section: Natural Strategies Of Ferredoxins For Thermostabilitymentioning

confidence: 99%

“…At the end of this paper, our structure is compared with another NMR structure of the same molecule published recently (Baumann et al, 1996), since their structure and discussion were totally different from ours.…”

Section: Introductionmentioning

confidence: 95%

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Hatanaka

Tanimura

Katoh

et al. 1997

Journal of Molecular Biology

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“…The average rmsd values between each component of the family and the mean structure for parsley Fd I (Table 6) show that the structure quality is much better than that of the recently reported solution structure of S. elongatus Fd I (rmsd of 0.87 Å for backbone and 1.30 Å for all heavy atoms) [21]. Residues 35Ϫ49 and 60Ϫ65 were reported to have the largest rmsd values in the solution structure of S. elongatus, as also found in the present case because of the paramagnetic region.…”

Section: Comparison With Other [2fe-2s] Structuresmentioning

confidence: 68%

“…The main secondary structure elements of parsley Fd I are the seven β-sheets sections 3Ϫ7, 16Ϫ 18, 49Ϫ51, 56Ϫ57, 73Ϫ74, 81Ϫ82 and 86Ϫ89, and four Ahelices at 24Ϫ30, 68Ϫ71, 76Ϫ78 and 92Ϫ95. Synechococcus elongatus Fd has six β-sheets and three A-helices [21]. The Ahelical region from 76 to 78 and the β-sheet region from 49 to 51 in parsley Fd I are not observed in the S. elongatus Fd.…”

Section: Comparison With Other [2fe-2s] Structuresmentioning

confidence: 88%

“…In the few NMR solution structures of oxidized [2Fe-2S]ferredoxins reported from Pseudomonas putida [19], Synechocystis sp. PCC 6803 [20] and Synechococcus elongatus [21], the quality of the structures is severely hampered by the lack of NOEs closer than about 8 Å from the iron atoms, as previously noted [22]. To achieve a reasonable folding it was necessary to introduce several bond distances and angles derived from the X-ray crystal structure for the [2Fe-2S] active centers as well as for nearby residues.…”

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confidence: 99%

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The solution structure of parsley [2Fe‐2S]ferredoxin

Liu

Luchinat

et al. 1998

European Journal of Biochemistry

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The [2Fe-2S]ferredoxin I (Fd I) from parsley leaves (M r ϭ 10500; 96 amino acids) in the Fe(III)-Fe(III) oxidized form has been studied by 1 H-NMR spectroscopy. Sequence-specific 1 H-NMR assignments were obtained through two-dimensional classical double-quantum-filtered-COSY, NOESY and TOCSY spectra. NOEs between protons as close as 5.6 Å from the paramagnetic Fe(III) atoms were observed at 800 MHz. A total of 3066 NOEs (of which 2533 are meaningful) and 18 distance constraints taken from X-ray crystallography of the Fe 2 S 2 active site were used to obtain the solution structure. From inversion recovery NOESY experiments, 33 longitudinal relaxation rate (AE para ) constraints were used for the structural refinement. The final structure was obtained by a process of restrained energy minimization. Root-mean-square (rmsd) deviation values obtained for the family of 18 structures (with reference to the average structure) are 0.52 Ϯ0.10 Å and 0.91Ϯ 0.12 Å for backbone and all heavy atoms respectively. The structure consists of seven-strands of β-sheets and four short A-helices. The quality of the present solution structure is among the best of those reported for [2Fe-2S]ferredoxins. The secondary structure and overall folding are compared with those of Anabaena variabilis Fd and the higher plant Equistum arvense (horse tail) protein determined through X-ray crystallography. The groups believed to be responsible for electron transfer have been analysed.Keywords : ferredoxin; solution structure; paramagnetism. Plant [2Fe-2S]ferredoxins are very important redox components involved in photosystem I (PSI) electron transport [1Ϫ3].They perform one-electron transfer (ET) from subunit PsaC of PSI to ferredoxin NADP-reductase (FNR), ferredoxin nitrite oxidoreductase, glutamate synthase and sulfite reductase [4]. There are now more than 75 amino acid sequences for this class of protein from higher plants, algae and cyanobacteria [1] (Table 1). Plant ferredoxins are very acidic (pI ϭ 3.4), with a charge balance of Ϫ18(Ϯ 2) at pH 7.5 from amino acid compositions. From X-ray crystallography on cyanobacteria PSI (6 Å resolution), it appears that the PSI subunits PsaD, PsaE and PsaC are involved in establishing an electrostatic orientation of the located on Fe(I), which is the Fe closest to the protein surface (Ϸ5 Å ) [17].The NMR technique is a powerful method for determining solution structures of small biomolecules. At first it was believed that it would be very difficult (or impossible) to detect a sufficiently large number of constraints for solution structure determination of paramagnetic metalloproteins. Since the first NMR solution structure of a paramagnetic protein in 1994 [18], new strategies and approaches have been introduced. In the few NMR solution structures of oxidized [2Fe-2S]ferredoxins reported from Pseudomonas putida [19], Synechocystis sp. PCC 6803 [20] and Synechococcus elongatus [21], the quality of the structures is severely hampered by the lack of NOEs closer than about 8 Å from the iron atoms, as previou...

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Structural alignment of ferredoxin and flavodoxin based on electrostatic potentials: Implications for their interactions with photosystem I and ferredoxin-NADP reductase

et al. 2000

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The two proteins ferredoxin and flavodoxin can replace each other in the photosynthetic electron transfer chain of cyanobacteria and algae. However, structure, size, and composition of ferredoxin and flavodoxin are completely different. Ferredoxin is a small iron-sulfur protein (ϳ100 amino acids), whereas flavodoxin is a flavin-containing protein (ϳ170 amino acids). The crystal structure of both proteins from the cyanobacteria Anabeana PCC 7120 is known. We used these two protein structures to investigate the structural basis of their functional equivalence. We apply the Hodgkin index to quantify the similarity of their electrostatic potentials. The technique has been applied successfully in indirect drug design for the alignment of small molecule and bioisosterism elucidation. It requires no predefined atom-atom correspondences. As is known from experiments, electrostatic interactions are most important for the association of ferredoxin and flavodoxin with their reaction partners photosystem I and ferredoxin-NADP reductase. Therefore, use of electrostatic potentials for the structural alignment is well justified. Our extensive search of the alignment space reveals two alignments with a high degree of similarity in the electrostatic potential. In both alignments, ferredoxin overlaps completely with flavodoxin. The active sites of ferredoxin and flavodoxin rather than their centers of mass coincide in both alignments. This is in agreement with electron microscopy investigations on photosystem I cross-linked to ferredoxin or flavodoxin. We identify residues that may have the same function in both proteins and relate our results to previous experimental data. Proteins 2000;38:301-309.

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Structure of Synechococcus elongatus [Fe₂S₂] Ferredoxin in Solution

Cited by 45 publications

References 46 publications

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

Solution structure of ferredoxin from the thermophilic Cyanobacterium Synechococcus elongatus and its thermostability

The solution structure of parsley [2Fe‐2S]ferredoxin

Structural alignment of ferredoxin and flavodoxin based on electrostatic potentials: Implications for their interactions with photosystem I and ferredoxin-NADP reductase

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