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'''CRYSTAL STRUCTURE OF LUXS''' | '''CRYSTAL STRUCTURE OF LUXS''' | ||
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[[Category: Hilgers, M T.]] | [[Category: Hilgers, M T.]] | ||
[[Category: Ludwig, M L.]] | [[Category: Ludwig, M L.]] | ||
[[Category: | [[Category: Cysteine-sulfonic acid]] | ||
[[Category: | [[Category: Four stranded antiparallel beta sheet]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Zinc]] | ||
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Revision as of 19:53, 2 May 2008
CRYSTAL STRUCTURE OF LUXS
OverviewOverview
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.
About this StructureAbout this Structure
1IE0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site., Hilgers MT, Ludwig ML, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11169-74. Epub 2001 Sep 11. PMID:11553770 Page seeded by OCA on Fri May 2 19:53:45 2008