1ie0: Difference between revisions

Revision as of 14:10, 21 February 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 with and as ligands. 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 Thu Feb 21 13:10:54 2008

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OCA

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-[[Image:1ie0.gif|left|200px]]<br /><applet load="1ie0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ie0.gif|left|200px]]<br /><applet load="1ie0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ie0, resolution 1.6&Aring;" />
 '''CRYSTAL STRUCTURE OF LUXS'''<br />
 ==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.
+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==
-IE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IE0 OCA].
+IE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE0 OCA].
 ==Reference==
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 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Hilgers, M.T.]]
+[[Category: Hilgers, M T.]]
-[[Category: Ludwig, M.L.]]
+[[Category: Ludwig, M L.]]
 [[Category: GOL]]
 [[Category: ZN]]
@@ Line 22: / Line 22: @@
 [[Category: zinc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:19:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:54 2008''