Structure of a Thioredoxin-like [2Fe-2S] Ferredoxin from Aquifex aeolicus
Abstract
The 2.3 Å resolution crystal structure of a [2Fe-2S] cluster containing ferredoxin from Aquifex aeolicusreveals 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.
Additional Information
© 2000 Academic Press. Received 29 March 2000; received in revised form 12 May 2000; accepted 15 May 2000. We thank the National Institutes of Health (D.C.R.) for support. A.P.Y. was supported in part by a National Science Foundation Graduate Research Fellowship. This work is based upon research conducted at the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the Department of Energy, Office of Basic Energy Sciences. The Biotechnology Program is supported by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program and the Department of Energy, Office of Biological and Environmental Research.Additional details
- Eprint ID
- 53413
- DOI
- 10.1006/jmbi.2000.3871
- Resolver ID
- CaltechAUTHORS:20150108-154426156
- NIH
- NSF Graduate Research Fellowship
- Department of Energy (DOE)
- Created
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2015-01-14Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field