1F37

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

Summary for 1F37

• Entry DOI: 10.2210/pdb1f37/pdb
• Descriptor: FERREDOXIN [2FE-2S], FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (4 entities in total)
• Functional Keywords: ferredoxin, [2fe-2s] cluster, thioredoxin fold, electron transport
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 2
• Total formula weight: 24948.14

Authors

Yeh, A.P.,Chatelet, C.,Soltis, S.M.,Kuhn, P.,Meyer, J.,Rees, D.C. (deposition date: 2000-05-31, release date: 2000-07-26, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)