1F37

STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS

1F37 の概要

• エントリーDOI: 10.2210/pdb1f37/pdb
• 分子名称: FERREDOXIN [2FE-2S], FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ferredoxin, [2fe-2s] cluster, thioredoxin fold, electron transport
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24948.14

構造登録者

Yeh, A.P.,Chatelet, C.,Soltis, S.M.,Kuhn, P.,Meyer, J.,Rees, D.C. (登録日: 2000-05-31, 公開日: 2000-07-26, 最終更新日: 2024-02-07)

主引用文献

Yeh, A.P.,Chatelet, C.,Soltis, S.M.,Kuhn, P.,Meyer, J.,Rees, D.C.
Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.
J.Mol.Biol., 300:587-595, 2000

PubMed Abstract: The 2.3 A resolution crystal structure of a [2Fe-2S] cluster containing ferredoxin from Aquifex aeolicus reveals a thioredoxin-like fold that is novel among iron-sulfur proteins. The [2Fe-2S] cluster is located near the surface of the protein, at a site corresponding to that of the active-site disulfide bridge in thioredoxin. The four cysteine ligands are located near the ends of two surface loops. Two of these ligands can be substituted by non-native cysteine residues introduced throughout a stretch of the polypeptide chain that forms a protruding loop extending away from the cluster. The presence of homologs of this ferredoxin as components of more complex anaerobic and aerobic electron transfer systems indicates that this is a versatile fold for biological redox processes.

PubMed: 10884354
DOI: 10.1006/jmbi.2000.3871

実験手法

X-RAY DIFFRACTION (2.3 Å)