The Crystal Structure of the Escherichia coli Autoinducer-2 Processing Protein LsrF |
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| Authors: | Zamia Diaz Karina B Xavier Stephen T Miller |
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| Institution: | 1. Department of Chemistry and Biochemistry, Swarthmore College, Swarthmore, Pennsylvania, United States of America.; 2. Instituto Gulbenkian de Ciência, Oeiras, Portugal.; 3. Instituto de Tecnologia Química e Biológica, Estação Agronómica Nacional, Oeiras, Portugal.;Duke University Medical Center, United States of America |
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| 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 (αβ)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. |
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