1f37

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spinqualitylabelsall models 1f37, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1F37 is a Single protein structure of sequence from Aquifex aeolicus with FES and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus., Yeh AP, Chatelet C, Soltis SM, Kuhn P, Meyer J, Rees DC, J Mol Biol. 2000 Jul 14;300(3):587-95. PMID:10884354[[Category: [2fe-2s] cluster]]

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