The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF

Diaz, Z.; Xavier, KB.; Miller, ST.

http://hdl.handle.net/10400.7/193

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Authors

Diaz, Z.

Xavier, KB.

Miller, ST.

Abstract(s)

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.

URI

http://hdl.handle.net/10400.7/193

Citation

Diaz, Z., Xavier, KB., Miller, ST. (2009). “The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF”. PLoS Genet. 4 (8): 1-10