1pfd: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
1PFD is a | 1PFD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Petroselinum_crispum Petroselinum crispum] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--nitrate_reductase Ferredoxin--nitrate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.7.2 1.7.7.2] Structure known Active Site: FES. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PFD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:27:55 2007'' | ||
