The Crystal Structure of the Escherichia coli Autoinducer-2 Processing Protein LsrF

Journal Article · Thu Jan 01 04:00:00 EST 2009 · PLoS One

DOI:https://doi.org/10.1371/journal.pone.0006820· OSTI ID:980624

Diaz, Z; Xavier, K; Miller, 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 (??)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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 980624
• Report Number(s): BNL--93542-2010-JA
• Journal Information: PLoS One, Journal Name: PLoS One Journal Issue: 8 Vol. 4
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
ALDOLASES
BACTERIA
CRYSTAL STRUCTURE
ESCHERICHIA COLI
GENES
LIGANDS
PROCESSING
PROTEINS
RESIDUES
SACCHARIDES
SALMONELLA TYPHIMURIUM
SIGNALS
TRANSPORT
national synchrotron light source