1CZP

ANABAENA PCC7119 [2FE-2S] FERREDOXIN IN THE REDUCED AND OXIXIZED STATE AT 1.17 A

1CZP の概要

• エントリーDOI: 10.2210/pdb1czp/pdb
• 関連するPDBエントリー: 1QT9
• 分子名称: FERREDOXIN I, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: [2fe-2s] protein, crystal reduced with dithionite, electron transport
• 由来する生物種: Nostoc sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21762.89

構造登録者

Morales, R.,Charon, M.H.,Frey, M. (登録日: 1999-09-06, 公開日: 2000-01-14, 最終更新日: 2023-08-09)

主引用文献

Morales, R.,Charon, M.H.,Hudry-Clergeon, G.,Petillot, Y.,Norager, S.,Medina, M.,Frey, M.
Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes.
Biochemistry, 38:15764-15773, 1999

PubMed Abstract: The chemical sequence of the [2Fe-2S] ferredoxin from the cyanobacterium AnabaenaPCC7119 (Fd7119) and its high-resolution X-ray structures in the oxidized and reduced states have been determined. The Fd7119 sequence is identical to that of the ferredoxin from the PCC7120 strain (Fd7120). X-ray diffraction data were collected at 100 K with an oxidized trigonal Fd7119 crystal, at 1.3 A resolution, and with an orthorhombic crystal, previously reduced with dithionite and flash frozen under anaerobic conditions, at 1.17 A resolution. The two molecular models were determined by molecular replacement with the [2Fe-2S] ferredoxin from the strain PCC7120 (Rypniewski, W. R., Breiter, D. R., Benning, M. M., Wesenberg, G., Oh, B.-H., Markley, J. L., Rayment, I., and Holden, H. M. (1991) Biochemistry 30, 4126-4131.) The final R-factors are 0. 140 (for the reduced crystal) and 0.138 (for the oxidized crystal). The [2Fe-2S] cluster appears as a significantly distorted lozenge in the reduced and oxidized redox states. The major conformational difference between the two redox forms concerns the peptide bond linking Cys46 and Ser47 which points its carbonyl oxygen away from the [2Fe-2S] cluster ("CO out") in the reduced molecule and toward it ("CO in") in the oxidized one. The "CO out" conformation could be the signature of the reduction of the iron atom Fe1, which is close to the molecular surface. Superposition of the three crystallographically independent molecules shows that the putative recognition site with the physiological partner (FNR) involves charged, hydrophobic residues and invariant water molecules.

PubMed: 10625442
DOI: 10.1021/bi991578s

実験手法

X-RAY DIFFRACTION (1.17 Å)