1pfd
From Proteopedia
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'''THE SOLUTION STRUCTURE OF HIGH PLANT PARSLEY [2FE-2S] FERREDOXIN, NMR, 18 STRUCTURES''' | '''THE SOLUTION STRUCTURE OF HIGH PLANT PARSLEY [2FE-2S] FERREDOXIN, NMR, 18 STRUCTURES''' | ||
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[[Category: Luchinat, C.]] | [[Category: Luchinat, C.]] | ||
[[Category: Sykes, A G.]] | [[Category: Sykes, A G.]] | ||
| - | [[Category: | + | [[Category: Electron transport]] |
| - | + | [[Category: Nuclear relaxation]] | |
| - | [[Category: | + | [[Category: Paramagnetism]] |
| - | [[Category: | + | [[Category: Solution structure]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:01:18 2008'' |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:01, 3 May 2008
THE SOLUTION STRUCTURE OF HIGH PLANT PARSLEY [2FE-2S] FERREDOXIN, NMR, 18 STRUCTURES
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 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
1PFD is a Single protein structure of sequence from Petroselinum crispum. Full crystallographic information is available from OCA.
Reference
The solution structure of parsley [2Fe-2S]ferredoxin., Im SC, Liu G, Luchinat C, Sykes AG, Bertini I, Eur J Biochem. 1998 Dec 1;258(2):465-77. PMID:9874213 Page seeded by OCA on Sat May 3 05:01:18 2008
