title: Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.
abstract: Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site.
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie de Paris, Paris, France.
authors.forename: Stephane
authors.initials: S
authors.lastname: Rety
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie de Paris, Paris, France.
authors.forename: Patrick
authors.initials: P
authors.lastname: Deschamps
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie de Paris, Paris, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Leulliot
mesh_terms: D000863:Antacids / Q000494:pharmacology*; D018929:Cell Culture Techniques; D003460:Crystallization; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014368:Tryptophanase / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D000863:Antacids; D029968:Escherichia coli Proteins; D014368:Tryptophanase
keywords: alkaline stress; protein purification; tryptophanase