1a70

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(New page: 200px<br /><applet load="1a70" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a70, resolution 1.7&Aring;" /> '''SPINACH FERREDOXIN'''...)
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[[Image:1a70.gif|left|200px]]<br /><applet load="1a70" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a70, resolution 1.7&Aring;" />
caption="1a70, resolution 1.7&Aring;" />
'''SPINACH FERREDOXIN'''<br />
'''SPINACH FERREDOXIN'''<br />
==Overview==
==Overview==
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Ferredoxin I (Fd I) from Spinacia oleracea is composed of 97 amino-acid, residues and a [2Fe-2S] cluster. The crystal structure of the E92K mutant, of Fd I was solved by molecular replacement and refined to an R factor of, 19.6% for 11755 reflections at 1.7 A resolution. The overall structure and, the active centre of spinach Fd is highly conserved with respect to, ferredoxins of known structure. The E92K mutation appears to disturb a, hydrogen-bond network which stabilizes the loop bearing the [2Fe-2S], cluster. This observation provides a rationale for the reduced, electron-transfer efficiency displayed by the E92K mutant. Inspection of, the crystal packing reveals that the side chain of Lys92 is engaged in an, intermolecular interaction with Asp26 of a symmetry-related molecule. This, feature may explain why only the mutant E92K and not wild-type Fd I could, be successfully crystallized.
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Ferredoxin I (Fd I) from Spinacia oleracea is composed of 97 amino-acid residues and a [2Fe-2S] cluster. The crystal structure of the E92K mutant of Fd I was solved by molecular replacement and refined to an R factor of 19.6% for 11755 reflections at 1.7 A resolution. The overall structure and the active centre of spinach Fd is highly conserved with respect to ferredoxins of known structure. The E92K mutation appears to disturb a hydrogen-bond network which stabilizes the loop bearing the [2Fe-2S] cluster. This observation provides a rationale for the reduced electron-transfer efficiency displayed by the E92K mutant. Inspection of the crystal packing reveals that the side chain of Lys92 is engaged in an intermolecular interaction with Asp26 of a symmetry-related molecule. This feature may explain why only the mutant E92K and not wild-type Fd I could be successfully crystallized.
==About this Structure==
==About this Structure==
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1A70 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A70 OCA].
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1A70 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A70 OCA].
==Reference==
==Reference==
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[[Category: photosynthesis]]
[[Category: photosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:39:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:32 2008''

Revision as of 09:41, 21 February 2008


1a70, resolution 1.7Å

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SPINACH FERREDOXIN

Overview

Ferredoxin I (Fd I) from Spinacia oleracea is composed of 97 amino-acid residues and a [2Fe-2S] cluster. The crystal structure of the E92K mutant of Fd I was solved by molecular replacement and refined to an R factor of 19.6% for 11755 reflections at 1.7 A resolution. The overall structure and the active centre of spinach Fd is highly conserved with respect to ferredoxins of known structure. The E92K mutation appears to disturb a hydrogen-bond network which stabilizes the loop bearing the [2Fe-2S] cluster. This observation provides a rationale for the reduced electron-transfer efficiency displayed by the E92K mutant. Inspection of the crystal packing reveals that the side chain of Lys92 is engaged in an intermolecular interaction with Asp26 of a symmetry-related molecule. This feature may explain why only the mutant E92K and not wild-type Fd I could be successfully crystallized.

About this Structure

1A70 is a Single protein structure of sequence from Spinacia oleracea with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution., Binda C, Coda A, Aliverti A, Zanetti G, Mattevi A, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1353-8. PMID:10089511

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