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New page: left|200px<br /><applet load="4fxc" size="450" color="white" frame="true" align="right" spinBox="true" caption="4fxc, resolution 2.5Å" /> '''TERTIARY STRUCTURE OF...
 
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[[Image:4fxc.jpg|left|200px]]<br /><applet load="4fxc" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:4fxc.jpg|left|200px]]<br /><applet load="4fxc" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="4fxc, resolution 2.5&Aring;" />
caption="4fxc, resolution 2.5&Aring;" />
'''TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS'''<br />
'''TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS'''<br />


==Overview==
==Overview==
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 &gt; 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.
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 &gt; 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.


==About this Structure==
==About this Structure==
4FXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entries 3FXC and 1FXC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4FXC OCA].  
4FXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entries 3FXC and 1FXC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXC OCA].  


==Reference==
==Reference==
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., Fukuyama K, Ueki N, Nakamura H, Tsukihara T, Matsubara H, J Biochem (Tokyo). 1995 May;117(5):1017-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8586613 8586613]
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., Fukuyama K, Ueki N, Nakamura H, Tsukihara T, Matsubara H, J Biochem. 1995 May;117(5):1017-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8586613 8586613]
[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: electron transport]]
[[Category: electron transport]]


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