1jvi: Difference between revisions

Revision as of 14:27, 21 February 2008

THE 2.2 ANGSTROM RESOLUTION STRUCTURE OF BACILLUS SUBTILIS LUXS/RIBOSILHOMOCYSTEINE COMPLEX

OverviewOverview

In bacteria, the regulation of gene expression in response to changes in cell density is called quorum sensing. The autoinducer-2 production protein LuxS, is involved in a novel quorum-sensing system and is thought to catalyse the degradation of S-ribosylhomocysteine to homocysteine and the autoinducer molecule 4,5-dihydroxy-2,3-pentadione. The crystal structure of Bacillus subtilis LuxS has been determined at 1.2 A resolution, together with the binary complexes of LuxS with S-ribosylhomocysteine and homocysteine to 2.2 and 2.3 A resolution, respectively. These structures show that LuxS is a homodimer with an apparently novel fold based on an eight-stranded beta-barrel, flanked by six alpha-helices. Each active site contains a zinc ion coordinated by the conserved residues His54, His58 and Cys126, and includes residues from both subunits. S-ribosylhomocysteine binds in a deep pocket with the ribose moiety adjacent to the enzyme-bound zinc ion. Access to the active site appears to be restricted and possibly requires conformational changes in the protein involving the movement of residues 125-129 and those at the N terminus. The structure contains an oxidised cysteine residue in the active site whose role in the biological process of LuxS has not been determined. The autoinducer-2 signalling pathway has been linked to aspects of bacterial virulence and pathogenicity. The structural data on LuxS will provide opportunities for targeting this enzyme for the rational design of new antibiotics.

About this StructureAbout this Structure

1JVI is a Single protein structure of sequence from Bacillus subtilis with , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis LuxS., Ruzheinikov SN, Das SK, Sedelnikova SE, Hartley A, Foster SJ, Horsburgh MJ, Cox AG, McCleod CW, Mekhalfia A, Blackburn GM, Rice DW, Baker PJ, J Mol Biol. 2001 Oct 12;313(1):111-22. PMID:11601850

Page seeded by OCA on Thu Feb 21 13:27:18 2008

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OCA

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-[[Image:1jvi.gif|left|200px]]<br /><applet load="1jvi" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jvi.gif|left|200px]]<br /><applet load="1jvi" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jvi, resolution 2.2&Aring;" />
 '''THE 2.2 ANGSTROM RESOLUTION STRUCTURE OF BACILLUS SUBTILIS LUXS/RIBOSILHOMOCYSTEINE COMPLEX'''<br />
 ==Overview==
-In bacteria, the regulation of gene expression in response to changes in, cell density is called quorum sensing. The autoinducer-2 production, protein LuxS, is involved in a novel quorum-sensing system and is thought, to catalyse the degradation of S-ribosylhomocysteine to homocysteine and, the autoinducer molecule 4,5-dihydroxy-2,3-pentadione. The crystal, structure of Bacillus subtilis LuxS has been determined at 1.2 A, resolution, together with the binary complexes of LuxS with, S-ribosylhomocysteine and homocysteine to 2.2 and 2.3 A resolution, respectively. These structures show that LuxS is a homodimer with an, apparently novel fold based on an eight-stranded beta-barrel, flanked by, six alpha-helices. Each active site contains a zinc ion coordinated by the, conserved residues His54, His58 and Cys126, and includes residues from, both subunits. S-ribosylhomocysteine binds in a deep pocket with the, ribose moiety adjacent to the enzyme-bound zinc ion. Access to the active, site appears to be restricted and possibly requires conformational changes, in the protein involving the movement of residues 125-129 and those at the, N terminus. The structure contains an oxidised cysteine residue in the, active site whose role in the biological process of LuxS has not been, determined. The autoinducer-2 signalling pathway has been linked to, aspects of bacterial virulence and pathogenicity. The structural data on, LuxS will provide opportunities for targeting this enzyme for the rational, design of new antibiotics.
+In bacteria, the regulation of gene expression in response to changes in cell density is called quorum sensing. The autoinducer-2 production protein LuxS, is involved in a novel quorum-sensing system and is thought to catalyse the degradation of S-ribosylhomocysteine to homocysteine and the autoinducer molecule 4,5-dihydroxy-2,3-pentadione. The crystal structure of Bacillus subtilis LuxS has been determined at 1.2 A resolution, together with the binary complexes of LuxS with S-ribosylhomocysteine and homocysteine to 2.2 and 2.3 A resolution, respectively. These structures show that LuxS is a homodimer with an apparently novel fold based on an eight-stranded beta-barrel, flanked by six alpha-helices. Each active site contains a zinc ion coordinated by the conserved residues His54, His58 and Cys126, and includes residues from both subunits. S-ribosylhomocysteine binds in a deep pocket with the ribose moiety adjacent to the enzyme-bound zinc ion. Access to the active site appears to be restricted and possibly requires conformational changes in the protein involving the movement of residues 125-129 and those at the N terminus. The structure contains an oxidised cysteine residue in the active site whose role in the biological process of LuxS has not been determined. The autoinducer-2 signalling pathway has been linked to aspects of bacterial virulence and pathogenicity. The structural data on LuxS will provide opportunities for targeting this enzyme for the rational design of new antibiotics.
 ==About this Structure==
-JVI 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, SO4, RHC and HCS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JVI OCA].
+JVI 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>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=RHC:'>RHC</scene> and <scene name='pdbligand=HCS:'>HCS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVI OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Baker, P.J.]]
+[[Category: Baker, P J.]]
-[[Category: Blackburn, G.M.]]
+[[Category: Blackburn, G M.]]
-[[Category: Cox, A.G.]]
+[[Category: Cox, A G.]]
-[[Category: Das, S.K.]]
+[[Category: Das, S K.]]
-[[Category: Foster, S.J.]]
+[[Category: Foster, S J.]]
 [[Category: Hartley, A.]]
-[[Category: Horsburgh, M.J.]]
+[[Category: Horsburgh, M J.]]
-[[Category: McCleod, C.W.]]
+[[Category: McCleod, C W.]]
 [[Category: Mekhalfia, A.]]
-[[Category: Rice, D.W.]]
+[[Category: Rice, D W.]]
-[[Category: Ruzheinikov, S.N.]]
+[[Category: Ruzheinikov, S N.]]
-[[Category: Sedelnikova, S.E.]]
+[[Category: Sedelnikova, S E.]]
 [[Category: HCS]]
 [[Category: RHC]]
@@ Line 31: / Line 31: @@
 [[Category: autoinducer synthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:36:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:18 2008''