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Article

Structural and biochemical study of effector molecule recognition by the E.coli glyoxylate and allantoin utilization regulatory protein AllR.

Journal of molecular biology - 5 May 2006

Walker John R, Altamentova Svetlana, Ezersky Alexandra, Lorca Graciela, Skarina Tatiana, Kudritska Marina, Ball Linda J, Bochkarev Alexey, Savchenko Alexei

Abstract excerpt

The interaction of Escherichia coli AllR regulator with operator DNA is disrupted by the effector molecule glyoxylate. This is a general, yet uncharacterized regulatory mechanism for the large IclR family of transcriptional regulators to which AllR belongs. The crystal structures of the C-terminal effector-binding domain of AllR regulator and its complex with glyoxylate were determined at 1.7 and 1.8 A,...

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PMID: 16546208
DOI: 10.1016/j.jmb.2006.02.034

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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