Crystallization and X-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enyme involved in siderophore biosynthesis.

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TitleCrystallization and X-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enyme involved in siderophore biosynthesis.
Publication TypeJournal Article
Year of Publication2006
AuthorsParsons, JF, Shi, K, Calabrese, K, Ladner, JE
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume62
IssuePt 3
Pagination271-4
Date Published2006 Mar 1
ISSN1744-3091
KeywordsChorismic Acid, Crystallization, Crystallography, X-Ray, Escherichia coli, Lyases, Siderophores
Abstract

Bacteria have evolved elaborate schemes that help them thrive in environments where free iron is severely limited. Siderophores such as yersiniabactin are small iron-scavenging molecules that are deployed by bacteria during iron starvation. Several studies have linked siderophore production and virulence. Yersiniabactin, produced by several Enterobacteriaceae, is derived from the key metabolic intermediate chorismic acid via its conversion to salicylate by salicylate synthase. Crystals of salicylate synthase from the uropathogen Escherichia coli CFT073 have been grown by vapour diffusion using polyethylene glycol as the precipitant. The monoclinic (P2(1)) crystals diffract to 2.5 A. The unit-cell parameters are a = 57.27, b = 164.07, c = 59.04 A, beta = 108.8 degrees. The solvent content of the crystals is 54% and there are two molecules of the 434-amino-acid protein in the asymmetric unit. It is anticipated that the structure will reveal key details about the reaction mechanism and the evolution of salicylate synthase.

DOI10.1107/S1744309106005677
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID16511320
PubMed Central IDPMC2197189