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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition.

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 A 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.[1]

References

  1. E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition. Williams, C.H., Stillman, T.J., Barynin, V.V., Sedelnikova, S.E., Tang, Y., Green, J., Guest, J.R., Artymiuk, P.J. Nat. Struct. Biol. (2002) [Pubmed]
 
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