NDLI: Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site

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Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hilgers, M. T. Ludwig, M. L.
Description	Author Affiliation: Hilgers MT ( Department of Biological Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109, USA.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Chemistry Metabolism Zinc Amidohydrolases Amino Acid Sequence Bacillus Subtilis Enzymology Binding Sites Carbon-Sulfur Lyases Cloning, Molecular Crystallography, X-Ray Endopeptidases Escherichia Coli Ligands Models, Molecular Molecular Sequence Data Protein Structure, Secondary Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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