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'''SPINACH FERREDOXIN''' | '''SPINACH FERREDOXIN''' | ||
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[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
[[Category: Zanetti, G.]] | [[Category: Zanetti, G.]] | ||
[[Category: | [[Category: Electron transport]] | ||
[[Category: | [[Category: Iron-sulfur protein]] | ||
[[Category: | [[Category: Photosynthesis]] | ||
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Revision as of 06:54, 2 May 2008
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. 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 Fri May 2 09:54:32 2008
