1PFD

THE SOLUTION STRUCTURE OF HIGH PLANT PARSLEY [2FE-2S] FERREDOXIN, NMR, 18 STRUCTURES

Summary for 1PFD

• Entry DOI: 10.2210/pdb1pfd/pdb
• NMR Information: BMRB: 4181
• Descriptor: FERREDOXIN, FE2/S2 (INORGANIC) CLUSTER (2 entities in total)
• Functional Keywords: [2fe-2s] ferredoxin, solution structure, paramagnetism, nuclear relaxation, electron transport
• Biological source: Petroselinum crispum (parsley)
• Total number of polymer chains: 1
• Total formula weight: 10672.20

Authors

Im, S.-C.,Liu, G.,Luchinat, C.,Sykes, A.G.,Bertini, I. (deposition date: 1998-05-05, release date: 1999-05-11, Last modification date: 2024-05-22)

Primary citation

Im, S.C.,Liu, G.,Luchinat, C.,Sykes, A.G.,Bertini, I.
The solution structure of parsley [2Fe-2S]ferredoxin.
Eur.J.Biochem., 258:465-477, 1998

PubMed Abstract: The [2Fe-2S]ferredoxin I (Fd I) from parsley leaves (Mr = 10,500; 96 amino acids) in the Fe(III)-Fe(III) oxidized form has been studied by 1H-NMR spectroscopy. Sequence-specific 1H-NMR assignments were obtained through two-dimensional classical double-quantum-filtered-COSY, NOESY and TOCSY spectra. NOEs between protons as close as 5.6 A 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 Fe2S2 active site were used to obtain the solution structure. From inversion recovery NOESY experiments, 33 longitudinal relaxation rate (Qpara) 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 +/- 0.10 A and 0.91 +/- 0.12 A for backbone and all heavy atoms respectively. The structure consists of seven-strands of beta-sheets and four short alpha-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.

PubMed: 9874213
DOI: 10.1046/j.1432-1327.1998.2580465.x

Experimental method

SOLUTION NMR