PMID:19714241

Citation	Diaz, Z, Xavier, KB and Miller, ST (2009) The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF. PLoS ONE 4:e6820
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 (alphabeta)(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.
Links	PubMed PMC2728841 Online version:10.1371/journal.pone.0006820
Keywords	4-Butyrolactone/analogs & derivatives; 4-Butyrolactone/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Catalytic Domain; Crystallization; Escherichia coli/metabolism; Ligands; Models, Molecular; Molecular Sequence Data; Protein Conformation; Salmonella typhimurium/metabolism; Sequence Homology, Amino Acid
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