This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a70

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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'''...)
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;" />
caption="1a70, resolution 1.7&Aring;" />
'''SPINACH FERREDOXIN'''<br />
'''SPINACH FERREDOXIN'''<br />
==Overview==
==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==
==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==
==Reference==
Line 23: Line 23:
[[Category: photosynthesis]]
[[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''

Revision as of 09:41, 21 February 2008


1a70, resolution 1.7Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 11:41:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools