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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/5860

Title: The Crystal Structure of the Escherichia coli Autoinducer-2 Processing Protein LsrF
Authors: Diaz, Z.
Xavier, K. B.
Miller, S. T.
Issue Date: 1-Jan-2009
Publisher: Public Library of Science
Abstract: Many bacteria produce and respond to the quorum sensing signal autoinducer-2 (AI-2). Escherichia coli and Salmonella typhimurium are among the species with the lsr operon, an operon containing AI-2 transport and processing genes that are up regulated in response to AI-2. One of the Lsr proteins, LsrF, has been implicated in processing the phosphorylated form of AI-2. Here, we present the structure of LsrF, unliganded and in complex with two phospho-AI-2 analogues, ribose-5-phosphate and ribulose-5-phosphate. The crystal structure shows that LsrF is a decamer of (alpha beta)(8)-barrels that exhibit a previously unseen N- terminal domain swap and have high structural homology with aldolases that process phosphorylated sugars. Ligand binding sites and key catalytic residues are structurally conserved, strongly implicating LsrF as a class I aldolase.
Description: PLOS ONE, 4(8):ARTe6820
URI: http://hdl.handle.net/10362/5860
ISSN: 1932-6203
Appears in Collections:ITQB: BS - Artigos em revista nacional com arbitragem científica

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