1a70: Difference between revisions

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[[Image:1a70.gif|left|200px]]<br /><applet load="1a70" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1a70.gif|left|200px]]<br /><applet load="1a70" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1a70, resolution 1.7Å" />

'''SPINACH FERREDOXIN'''<br />

==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.

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 [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].

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==

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[[Category: photosynthesis]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 10~~:39:~~02 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:32 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1a70.gif|left|200px]]<br /><applet load="1a70" size="450" color="white" frame="true" align="right" spinBox="true"
+[[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;" />
 '''SPINACH FERREDOXIN'''<br />
 ==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.
+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==
-A70 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].
+A70 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==
@@ Line 23: / Line 23: @@
 [[Category: photosynthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:39:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:32 2008''