1A70

SPINACH FERREDOXIN

Summary for 1A70

• Entry DOI: 10.2210/pdb1a70/pdb
• Descriptor: FERREDOXIN, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• Functional Keywords: iron-sulfur protein, photosynthesis, electron transport
• Biological source: Spinacia oleracea (spinach)
• Cellular location: Plastid, chloroplast: P00221
• Total number of polymer chains: 1
• Total formula weight: 10664.29

Authors

Binda, C.,Coda, A.,Mattevi, A.,Aliverti, A.,Zanetti, G. (deposition date: 1998-03-19, release date: 1998-11-25, Last modification date: 2024-05-22)

Primary citation

Binda, C.,Coda, A.,Aliverti, A.,Zanetti, G.,Mattevi, A.
Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution.
Acta Crystallogr.,Sect.D, 54:1353-1358, 1998

PubMed Abstract: 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.

PubMed: 10089511
DOI: 10.1107/S0907444998005137

Experimental method

X-RAY DIFFRACTION (1.7 Å)