1TM2

Crystal Structure of the apo form of the Salmonella typhimurium AI-2 receptor LsrB

Summary for 1TM2

• Entry DOI: 10.2210/pdb1tm2/pdb
• Related: 1JX6 1TJY
• Descriptor: sugar transport protein (2 entities in total)
• Functional Keywords: periplasmic binding protein, signaling protein
• Biological source: Salmonella typhimurium
• Cellular location: Periplasm : Q8Z2X8
• Total number of polymer chains: 1
• Total formula weight: 34250.65

Authors

Miller, S.T.,Xavier, K.B.,Campagna, S.R.,Taga, M.E.,Semmelhack, M.F.,Bassler, B.L.,Hughson, F.M. (deposition date: 2004-06-10, release date: 2004-09-28, Last modification date: 2024-11-06)

Primary citation

Miller, S.T.,Xavier, K.B.,Campagna, S.R.,Taga, M.E.,Semmelhack, M.F.,Bassler, B.L.,Hughson, F.M.
Salmonella typhimurium Recognizes a Chemically Distinct Form of the Bacterial Quorum-Sensing Signal AI-2
Mol.Cell, 15:677-687, 2004

PubMed Abstract: Bacterial populations use cell-cell communication to coordinate community-wide regulation of processes such as biofilm formation, virulence, and bioluminescence. This phenomenon, termed quorum sensing, is mediated by small molecule signals known as autoinducers. While most autoinducers are species specific, autoinducer-2 (AI-2), first identified in the marine bacterium Vibrio harveyi, is produced and detected by many Gram-negative and Gram-positive bacteria. The crystal structure of the V. harveyi AI-2 signaling molecule bound to its receptor protein revealed an unusual furanosyl borate diester. Here, we present the crystal structure of a second AI-2 signal binding protein, LsrB from Salmonella typhimurium. We find that LsrB binds a chemically distinct form of the AI-2 signal, (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran (R-THMF), that lacks boron. Our results demonstrate that two different species of bacteria recognize two different forms of the autoinducer signal, both derived from 4,5-dihydroxy-2,3-pentanedione (DPD), and reveal new sophistication in the chemical lexicon used by bacteria in interspecies signaling.

PubMed: 15350213
DOI: 10.1016/j.molcel.2004.07.020

Experimental method

X-RAY DIFFRACTION (1.9 Å)