4fxc

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[[Image:4fxc.jpg|left|200px]]
[[Image:4fxc.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_4fxc| PDB=4fxc | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxc OCA], [http://www.ebi.ac.uk/pdbsum/4fxc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4fxc RCSB]</span>
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'''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'''
'''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'''
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==About this Structure==
==About this Structure==
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4FXC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. 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].
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4FXC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1fxc 1fxc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXC OCA].
==Reference==
==Reference==
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[[Category: Fukuyama, K.]]
[[Category: Fukuyama, K.]]
[[Category: Tsukihara, T.]]
[[Category: Tsukihara, T.]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:48 2008''
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Revision as of 19:24, 4 May 2008

Template:STRUCTURE 4fxc

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


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 > 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

4FXC is a Single protein structure of sequence from Arthrospira platensis. This structure supersedes the now removed PDB entries and 1fxc. Full crystallographic information is available from OCA.

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. 1995 May;117(5):1017-23. PMID:8586613 Page seeded by OCA on Sun May 4 22:24:15 2008

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