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1f37
From Proteopedia
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| , resolution 2.3Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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]]
Page seeded by OCA on Thu Mar 20 11:03:46 2008
Categories: Aquifex aeolicus | Single protein | Chatelet, C. | Kuhn, P. | Meyer, J. | Rees, D C. | Soltis, S M. | Yeh, A P. | FES | GOL | Ferredoxin | Thioredoxin fold
