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

Abstract

Salicylate synthase, which catalyzes the first step in the synthesis of the siderophore yersiniabactin, has been crystallized. Diffraction data have been collected to 2.5 Å. 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{sub 1}) crystals diffract to 2.5 Å. The unit-cell parameters are a = 57.27, b = 164.07, c = 59.04 Å, β = 108.8°. 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.

Authors:
; ;  [1];  [1];  [2]
  1. Center for Advanced Research in Biotechnology, The University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850 (United States)
  2. (United States)
Publication Date:
OSTI Identifier:
22356300
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 3; Other Information: PMCID: PMC2197189; PMID: 16511320; PUBLISHER-ID: ll5050; OAI: oai:pubmedcentral.nih.gov:2197189; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CONVERSION; CRYSTALLIZATION; CRYSTALS; DIFFUSION; ENVIRONMENT; ESCHERICHIA COLI; EVOLUTION; IRON; MOLECULES; PROTEINS; REACTION KINETICS; SOLVENTS; X-RAY DIFFRACTION

Citation Formats

Parsons, James F., E-mail: parsonsj@umbi.umd.edu, Shi, Katherine, Calabrese, Kelly, Ladner, Jane E., and National Institute of Standards and Technology. Crystallization and X-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enyme involved in siderophore biosynthesis. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106005677.
Parsons, James F., E-mail: parsonsj@umbi.umd.edu, Shi, Katherine, Calabrese, Kelly, Ladner, Jane E., & National Institute of Standards and Technology. Crystallization and X-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enyme involved in siderophore biosynthesis. United Kingdom. doi:10.1107/S1744309106005677.
Parsons, James F., E-mail: parsonsj@umbi.umd.edu, Shi, Katherine, Calabrese, Kelly, Ladner, Jane E., and National Institute of Standards and Technology. Wed . "Crystallization and X-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enyme involved in siderophore biosynthesis". United Kingdom. doi:10.1107/S1744309106005677.
@article{osti_22356300,
title = {Crystallization and X-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enyme involved in siderophore biosynthesis},
author = {Parsons, James F., E-mail: parsonsj@umbi.umd.edu and Shi, Katherine and Calabrese, Kelly and Ladner, Jane E. and National Institute of Standards and Technology},
abstractNote = {Salicylate synthase, which catalyzes the first step in the synthesis of the siderophore yersiniabactin, has been crystallized. Diffraction data have been collected to 2.5 Å. 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{sub 1}) crystals diffract to 2.5 Å. The unit-cell parameters are a = 57.27, b = 164.07, c = 59.04 Å, β = 108.8°. 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.},
doi = {10.1107/S1744309106005677},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 62,
place = {United Kingdom},
year = {Wed Mar 01 00:00:00 EST 2006},
month = {Wed Mar 01 00:00:00 EST 2006}
}
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