Abstract
The major bifunctional aconitase of Escherichia coli (AcnB) serves as either an enzymic catalyst or a mRNA-binding post-transcriptional regulator, depending on the status of its iron–sulfur cluster. AcnB represents a large, distinct group of Gram-negative bacterial aconitases that have an altered domain organization relative to mitochondrial aconitase and other aconitases. Here the 2.4 Å structure of E. coli AcnB reveals a high degree of conservation at the active site despite its domain reorganization. It also reveals that the additional domain, characteristic of the AcnB subfamily, is a HEAT-like domain, implying a role in protein–protein recognition. This domain packs against the remainder of the protein to form a tunnel leading to the aconitase active site, potentially for substrate channeling.
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Acknowledgements
We thank BBSRC, EPSRC and the Wellcome Trust for their support, CCLRC Daresbury for synchrotron radiation facilities, and the Royal Society and Wolfson Foundation for computing facilities. The Krebs Institute is a BBSRC-designated Biomolecular Sciences center and a member of the North of England Structural Biology Centre.
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Williams, C., Stillman, T., Barynin, V. et al. E. coli aconitase B structure reveals a HEAT-like domain with implications for protein–protein recognition. Nat Struct Mol Biol 9, 447–452 (2002). https://doi.org/10.1038/nsb801
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DOI: https://doi.org/10.1038/nsb801
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