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Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal.
Open accessAbstract
The structure of activated pig heart aconitase [citrate(isocitrate) hydro-lyase, EC 4.2.1.3] containing a [4Fe-4S] cluster has been refined at 2.5-A resolution to a crystallographic residual of 18.2%. Comparison of this structure to the recently determined 2.1-A resolution structure of the inactive enzyme containing a [3Fe-4S] cluster, by difference Fourier analysis, shows that upon activation iron is inserted into the structure isomorphously. The common atoms of the [3Fe-4S] and [4Fe-4S] cores agree within 0.1 A; the three common cysteinyl S gamma ligand atoms agree within 0.25 A. The fourth ligand of the Fe inserted into the [3Fe-4S] cluster is a water or hydroxyl from solvent, consistent with the absence of a free cysteine ligand in the enzyme active site cleft and the isomorphism of the two structures. A water molecule occupies a similar site in the crystal structure of the inactive enzyme.
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Cited by
A new family of mesoporous molecular sieves prepared with liquid crystal templates
Beck, J. S., Vartuli, J. C., Roth, W. J., Leonowicz, M. E., Kresge, C. T., Schmitt, K. D., Chu, C. T. W., Olson, D. H., Sheppard, E. W., McCullen, S. B., et al. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00053a020 · Cited by 10,967
Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292
The inactivation of Fe-S cluster containing hydro-lyases by superoxide
Flint, D. H., Tuminello, J. F., & Emptage, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41538-4 · Cited by 637
Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606
Self-citationAconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.
Castro, L., Rodriguez, M., & Radi, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43894-x · Cited by 589
Metadata
- Authors
- Robbins, A. H., & Stout, C. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1989-05
- Volume
- 86
- Issue
- 10
- Pages
- 3639-3643
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2068022490
- Cited by
- 244
- References
- 0
- FWCI
- 24.46
- Type
- journal article
- Language
- en
- Open access
- green
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- Robbins, A. H., & Stout, C. D. (1989). Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.10.3639
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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