1ie0
From Proteopedia
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| - | [[Image:1ie0.gif|left|200px]] | + | [[Image:1ie0.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF LUXS''' | + | {{Structure |
| + | |PDB= 1ie0 |SIZE=350|CAPTION= <scene name='initialview01'>1ie0</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= LUXS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF LUXS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IE0 is a [ | + | 1IE0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE0 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11553770 11553770] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cysteine-sulfonic acid]] | [[Category: cysteine-sulfonic acid]] | ||
[[Category: four stranded antiparallel beta sheet]] | [[Category: four stranded antiparallel beta sheet]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:07 2008'' |
Revision as of 09:49, 20 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | LUXS (Bacillus subtilis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF LUXS
Overview
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 Structure
1IE0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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
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