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

PLoS One. 2009 Aug 28;4(8):e6820. doi: 10.1371/journal.pone.0006820.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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

Substances

  • Bacterial Proteins
  • Ligands
  • N-(3-oxohexanoyl)-3-aminodihydro-2(3H)-furanone
  • 4-Butyrolactone