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PMID: 11553770 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

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

Hilgers MT, Ludwig ML

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.

MeSH Terms
Amidohydrolases/chemistry Amino Acid Sequence Bacillus subtilis/enzymology Bacterial Proteins/chemistry,metabolism Binding Sites Carbon-Sulfur Lyases Cloning, Molecular Crystallography, X-Ray Endopeptidases/chemistry Escherichia coli Ligands Models, Molecular Molecular Sequence Data Protein Structure, Secondary Recombinant Proteins/chemistry,metabolism Sequence Alignment Sequence Homology, Amino Acid Zinc/metabolism
Chemicals
Bacterial Proteins Ligands Recombinant Proteins Endopeptidases Amidohydrolases Carbon-Sulfur Lyases LuxS protein, Bacteria Zinc
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hilgers M T
Department of Biological Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109, USA.
Ludwig M L
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2001-09-25
Epub
2001-00-11
Pages
11169-74
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC58702
Subset
IM
Grants
NIGMS NIH HHS · R01 GM016429 · United States
NIGMS NIH HHS · T32 GM008270 · United States
NIGMS NIH HHS · GM 08270 · United States
NIGMS NIH HHS · GM 16429 · United States
Databases
PDB
Analysis Services
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