Structural highlights
Function
[ACON2_ECOLI] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition.,Williams CH, Stillman TJ, Barynin VV, Sedelnikova SE, Tang Y, Green J, Guest JR, Artymiuk PJ Nat Struct Biol. 2002 Jun;9(6):447-52. PMID:11992126[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Williams CH, Stillman TJ, Barynin VV, Sedelnikova SE, Tang Y, Green J, Guest JR, Artymiuk PJ. E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition. Nat Struct Biol. 2002 Jun;9(6):447-52. PMID:11992126 doi:10.1038/nsb801
