1IE0

CRYSTAL STRUCTURE OF LUXS

Summary for 1IE0

• Entry DOI: 10.2210/pdb1ie0/pdb
• Descriptor: AUTOINDUCER-2 PRODUCTION PROTEIN LUXS, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: four stranded antiparallel beta sheet, cysteine-sulfonic acid, structural genomics
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 17943.73

Authors

Hilgers, M.T.,Ludwig, M.L. (deposition date: 2001-04-05, release date: 2001-10-03, Last modification date: 2025-03-26)

Primary citation

Hilgers, M.T.,Ludwig, M.L.
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site.
Proc.Natl.Acad.Sci.USA, 98:11169-11174, 2001

PubMed Abstract: The ability of bacteria to regulate gene expression in response to changes in cell density is termed quorum sensing. This behavior involves the synthesis and recognition of extracellular, hormone-like compounds known as autoinducers. Here we report the structure of an autoinducer synthase, LuxS from Bacillus subtilis, at 1.6-A resolution (R(free) = 0.204; R(work) = 0.174). LuxS is a homodimeric enzyme with a novel fold that incorporates two identical tetrahedral metal-binding sites. This metal center is composed of a Zn(2+) atom coordinated by two histidines, a cysteine, and a solvent molecule, and is reminiscent of active sites found in several peptidases and amidases. Although the nature of the autoinducer synthesized by LuxS cannot be deduced from the crystal structure, features of the putative active site suggest that LuxS might catalyze hydrolytic, but not proteolytic, cleavage of a small substrate. Our analysis represents a test of structure-based functional assignment.

PubMed: 11553770
DOI: 10.1073/pnas.191223098

Experimental method

X-RAY DIFFRACTION (1.6 Å)