Schmelz, Stefan, Kadi, N., McMahon, Stephen A., Song, Lijiang, Oves-Costales, Daniel, Oke, Muse, Liu, Huanting, Johnson, K. A. (Kenneth A.), Carter, Lester G., Botting, Catherine H., White, Malcolm F., Challis, Gregory L. and Naismith, James H.. (2009) AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis. Nature Chemical Biology, Vol.5 (No.3). pp. 174-182. ISSN 1552-4450

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Abstract

Bacterial pathogens need to scavenge iron from their host for growth and proliferation during infection. They have evolved several strategies to do this, one being the biosynthesis and excretion of small, high-affinity iron chelators known as siderophores. The biosynthesis of siderophores is an important area of study, not only for potential therapeutic intervention but also to illuminate new enzyme chemistries. Two general pathways for siderophore biosynthesis exist: the well-characterized nonribosomal peptide synthetase (NRPS)-dependent pathway and the NRPS-independent siderophore (NIS) pathway, which relies on a different family of sparsely investigated synthetases. Here we report structural and biochemical studies of AcsD from Pectobacterium (formerly Erwinia) chrysanthemi, an NIS synthetase involved in achromobactin biosynthesis. The structures of ATP and citrate complexes provide a mechanistic rationale for stereospecific formation of an enzyme-bound (3R)-citryladenylate, which reacts with L-serine to form a likely achromobactin precursor. AcsD is a unique acyladenylate-forming enzyme with a new fold and chemical catalysis strategy.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Siderophores -- Synthesis, Pathogenic microorganisms, Enantioselective catalysis, Protein kinases, Enzymes
Journal or Publication Title:	Nature Chemical Biology
Publisher:	Nature Publishing Group
ISSN:	1552-4450
Official Date:	March 2009
Dates:	Date Event March 2009 Published
Volume:	Vol.5
Number:	No.3
Number of Pages:	9
Page Range:	pp. 174-182
Identification Number:	10.1038/nchembio.145
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Scottish Funding Council (SFC)
Grant number:	BB/S/B14450 (BBSRC)
URI:	http://wrap.warwick.ac.uk/id/eprint/28457

Data sourced from Thomson Reuters' Web of Knowledge

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