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Article

Structural analysis of ligand binding and catalysis in chorismate lyase.

Archives of biochemistry and biophysics - 1 Jan 2006

Smith Natasha, Roitberg Adrian E, Rivera Eva, Howard Andrew, Holden Marcia J, Mayhew Martin, Kaistha Salita, Gallagher D T

Abstract excerpt

Chorismate lyase (CL) removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. We previously reported the crystal structure at 1.4A resolution of the Escherichia coli CL with bound 4HB product, showing that the product is bound in an internal cavity behind two flaps. To provide a more complete basis for understanding CL's unusual ligand-binding properties and...

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Identifiers

PMID: 16343413
DOI: 10.1016/j.abb.2005.10.026

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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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