http://hdl.handle.net/10362/3688 2013-06-20T07:42:29Z 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. 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 2009-01-01T00:00:00Z