Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.

Autor: Yeh AP; Division of Chemistry and Chemical Engineering 147-75CH, California Institute of Technology, Pasadena, CA, 91125, USA., Chatelet C, Soltis SM, Kuhn P, Meyer J, Rees DC
Jazyk: angličtina
Zdroj: Journal of molecular biology [J Mol Biol] 2000 Jul 14; Vol. 300 (3), pp. 587-95.
DOI: 10.1006/jmbi.2000.3871
Abstrakt: 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.
(Copyright 2000 Academic Press.)
Databáze: MEDLINE
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