PMID:11992126
| Citation |
Williams, CH, Stillman, TJ, Barynin, VV, Sedelnikova, SE, Tang, Y, Green, J, Guest, JR and Artymiuk, PJ (2002) E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition. Nat. Struct. Biol. 9:447-52 |
|---|---|
| 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 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. |
| Links |
PubMed Online version:10.1038/nsb801 |
| Keywords |
Aconitate Hydratase/chemistry; Aconitate Hydratase/metabolism; Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites; Cattle; Conserved Sequence; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; Protein Binding; Protein Structure, Tertiary; RNA/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/metabolism; Sequence Alignment; Structure-Activity Relationship |
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