3GLC

Crystal Structure of E. coli LsrF in complex with Ribose-5-phosphate

Summary for 3GLC

• Entry DOI: 10.2210/pdb3glc/pdb
• Related: 3GKF 3GND
• Descriptor: Aldolase lsrF, RIBOSE-5-PHOSPHATE (3 entities in total)
• Functional Keywords: tim barrel, lyase, schiff base
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Potential): P76143
• Total number of polymer chains: 20
• Total formula weight: 651045.10

Authors

Miller, S.T.,Diaz, Z.C. (deposition date: 2009-03-11, release date: 2009-09-08, Last modification date: 2023-09-06)

Primary citation

Diaz, Z.,Xavier, K.B.,Miller, S.T.
The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF.
Plos One, 4:e6820-e6820, 2009

PubMed 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.

PubMed: 19714241
DOI: 10.1371/journal.pone.0006820

Experimental method

X-RAY DIFFRACTION (2.5 Å)