1L5J

CRYSTAL STRUCTURE OF E. COLI ACONITASE B.

Summary for 1L5J

• Entry DOI: 10.2210/pdb1l5j/pdb
• Descriptor: Aconitate hydratase 2, ACONITATE ION, FE3-S4 CLUSTER, ... (4 entities in total)
• Functional Keywords: molecular recognition, rna binding, citric acid cycle, heat-like domain, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 188135.52

Authors

Williams, C.H.,Stillman, T.J.,Barynin, V.V.,Sedelnikova, S.E.,Tang, Y.,Green, J.,Guest, J.R.,Artymiuk, P.J. (deposition date: 2002-03-07, release date: 2002-06-12, Last modification date: 2024-02-14)

Primary citation

Williams, C.H.,Stillman, T.J.,Barynin, V.V.,Sedelnikova, S.E.,Tang, Y.,Green, J.,Guest, J.R.,Artymiuk, P.J.
E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition.
Nat.Struct.Biol., 9:447-452, 2002

PubMed 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.

PubMed: 11992126
DOI: 10.1038/nsb801

Experimental method

X-RAY DIFFRACTION (2.4 Å)