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The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site
Authors
Adams
Atkins
+43 more
Butty
Cameron
Caroff
Cuccui
Davis
De Leon
DeShazer
Emsley
Evans
Holliday
Hsueh
Jenney
John
Langer
Larkin
Lazar Adler
Leslie
McCoy
Mizuguchi
Nelson
Ngauy
Nicholas J. Harmer
Overington
Pacinelli
Painter
Pape
Raetz
Reckseidler
Reckseidler-Zenteno
Rotz
Seetharaman
Sheldrick
St. Michael
Stone
Studier
Taylor
Taylor
Valvano
Vonrhein
Warawa
White
Whitfield
Wiersinga
Publication date
31 May 2013
Publisher
'Elsevier BV'
Doi
Cite
Abstract
Copyright © 2010 Elsevier. NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Molecular Biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Biology, 2010, Vol. 400, Issue 3, pp. 379 – 392 DOI: http://dx.doi.org/10.1016/j.jmb.2010.04.058Heptoses are found in the surface polysaccharides of most bacteria, contributing to structures that are essential for virulence and antibiotic resistance. Consequently, the biosynthetic enzymes for these sugars are attractive targets for novel antibiotics. The best characterized biosynthetic enzyme is GmhA, which catalyzes the conversion of sedoheptulose-7-phosphate into D-glycero-D-manno-heptopyranose-7-phosphate, the first step in the biosynthesis of heptose. Here, the structure of GmhA from Burkholderia pseudomallei is reported. This enzyme contains a zinc ion at the heart of its active site: this ion stabilizes the active, closed form of the enzyme and presents coordinating side chains as a potential acid and base to drive catalysis. A complex with the product demonstrates that the enzyme retains activity in the crystal and thus suggests that the closed conformation is catalytically relevant and is an excellent target for the development of therapeutics. A revised mechanism for the action of GmhA is postulated on the basis of this structure and the activity of B. pseudomallei GmhA mutants
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Last time updated on 06/08/2013
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