1inn: Difference between revisions

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[[Image:1inn.jpg|left|200px]]<br /><applet load="1inn" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1inn.jpg|left|200px]]<br /><applet load="1inn" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1inn, resolution 1.80Å" />

'''CRYSTAL STRUCTURE OF D. RADIODURANS LUXS, P21'''<br />

==Overview==

BACKGROUND: Quorum sensing is the mechanism by which bacteria control gene, expression in response to cell density. Two major quorum-sensing systems, have been identified, system 1 and system 2, each with a characteristic, signaling molecule (autoinducer-1, or AI-1, in the case of system 1, and, AI-2 in system 2). The luxS gene is required for the AI-2 system of quorum, sensing. LuxS and AI-2 have been described in both Gram-negative and, Gram-positive bacterial species and have been shown to be involved in the, expression of virulence genes in several pathogens. RESULTS: The structure, of the LuxS protein from three different bacterial species with, resolutions ranging from 1.8 A to 2.4 A has been solved using an X-ray, crystallographic structural genomics approach. The structure of LuxS, reported here is seen to have a new alpha-beta fold. In all structures, an, equivalent homodimer is observed. A metal ion identified as zinc was seen, bound to a Cys-His-His triad. Methionine was found bound to the protein, near the metal and at the dimer interface. CONCLUSIONS: These structures, provide support for a hypothesis that explains the in vivo action of LuxS., Specifically, acting as a homodimer, the protein binds a methionine, analog, S-ribosylhomocysteine (SRH). The zinc atom is in position to, cleave the ribose ring in a step along the synthesis pathway of AI-2.

BACKGROUND: Quorum sensing is the mechanism by which bacteria control gene expression in response to cell density. Two major quorum-sensing systems have been identified, system 1 and system 2, each with a characteristic signaling molecule (autoinducer-1, or AI-1, in the case of system 1, and AI-2 in system 2). The luxS gene is required for the AI-2 system of quorum sensing. LuxS and AI-2 have been described in both Gram-negative and Gram-positive bacterial species and have been shown to be involved in the expression of virulence genes in several pathogens. RESULTS: The structure of the LuxS protein from three different bacterial species with resolutions ranging from 1.8 A to 2.4 A has been solved using an X-ray crystallographic structural genomics approach. The structure of LuxS reported here is seen to have a new alpha-beta fold. In all structures, an equivalent homodimer is observed. A metal ion identified as zinc was seen bound to a Cys-His-His triad. Methionine was found bound to the protein near the metal and at the dimer interface. CONCLUSIONS: These structures provide support for a hypothesis that explains the in vivo action of LuxS. Specifically, acting as a homodimer, the protein binds a methionine analog, S-ribosylhomocysteine (SRH). The zinc atom is in position to cleave the ribose ring in a step along the synthesis pathway of AI-2.

==About this Structure==

1INN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with ZN and MET as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1INN OCA].

1INN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MET:'>MET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INN OCA].

==Reference==

Line 13:

[[Category: Deinococcus radiodurans]]

[[Category: Single protein]]

[[Category: Bergseid, M.G.]]

[[Category: Bergseid, M G.]]

[[Category: Buchanan, S.G.]]

[[Category: Buchanan, S G.]]

[[Category: Furlong, E.B.]]

[[Category: Furlong, E B.]]

[[Category: Lewis, H.A.]]

[[Category: Lewis, H A.]]

[[Category: Sanderson, W.E.]]

[[Category: Sanderson, W E.]]

[[Category: MET]]

[[Category: ZN]]

[[Category: alpha-beta fold]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1inn.jpg|left|200px]]<br /><applet load="1inn" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1inn.jpg|left|200px]]<br /><applet load="1inn" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1inn, resolution 1.80&Aring;" />
 '''CRYSTAL STRUCTURE OF D. RADIODURANS LUXS, P21'''<br />
 ==Overview==
-BACKGROUND: Quorum sensing is the mechanism by which bacteria control gene, expression in response to cell density. Two major quorum-sensing systems, have been identified, system 1 and system 2, each with a characteristic, signaling molecule (autoinducer-1, or AI-1, in the case of system 1, and, AI-2 in system 2). The luxS gene is required for the AI-2 system of quorum, sensing. LuxS and AI-2 have been described in both Gram-negative and, Gram-positive bacterial species and have been shown to be involved in the, expression of virulence genes in several pathogens. RESULTS: The structure, of the LuxS protein from three different bacterial species with, resolutions ranging from 1.8 A to 2.4 A has been solved using an X-ray, crystallographic structural genomics approach. The structure of LuxS, reported here is seen to have a new alpha-beta fold. In all structures, an, equivalent homodimer is observed. A metal ion identified as zinc was seen, bound to a Cys-His-His triad. Methionine was found bound to the protein, near the metal and at the dimer interface. CONCLUSIONS: These structures, provide support for a hypothesis that explains the in vivo action of LuxS., Specifically, acting as a homodimer, the protein binds a methionine, analog, S-ribosylhomocysteine (SRH). The zinc atom is in position to, cleave the ribose ring in a step along the synthesis pathway of AI-2.
+BACKGROUND: Quorum sensing is the mechanism by which bacteria control gene expression in response to cell density. Two major quorum-sensing systems have been identified, system 1 and system 2, each with a characteristic signaling molecule (autoinducer-1, or AI-1, in the case of system 1, and AI-2 in system 2). The luxS gene is required for the AI-2 system of quorum sensing. LuxS and AI-2 have been described in both Gram-negative and Gram-positive bacterial species and have been shown to be involved in the expression of virulence genes in several pathogens. RESULTS: The structure of the LuxS protein from three different bacterial species with resolutions ranging from 1.8 A to 2.4 A has been solved using an X-ray crystallographic structural genomics approach. The structure of LuxS reported here is seen to have a new alpha-beta fold. In all structures, an equivalent homodimer is observed. A metal ion identified as zinc was seen bound to a Cys-His-His triad. Methionine was found bound to the protein near the metal and at the dimer interface. CONCLUSIONS: These structures provide support for a hypothesis that explains the in vivo action of LuxS. Specifically, acting as a homodimer, the protein binds a methionine analog, S-ribosylhomocysteine (SRH). The zinc atom is in position to cleave the ribose ring in a step along the synthesis pathway of AI-2.
 ==About this Structure==
-INN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with ZN and MET as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1INN OCA].
+INN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MET:'>MET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INN OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Deinococcus radiodurans]]
 [[Category: Single protein]]
-[[Category: Bergseid, M.G.]]
+[[Category: Bergseid, M G.]]
-[[Category: Buchanan, S.G.]]
+[[Category: Buchanan, S G.]]
-[[Category: Furlong, E.B.]]
+[[Category: Furlong, E B.]]
-[[Category: Lewis, H.A.]]
+[[Category: Lewis, H A.]]
-[[Category: Sanderson, W.E.]]
+[[Category: Sanderson, W E.]]
 [[Category: MET]]
 [[Category: ZN]]
 [[Category: alpha-beta fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:31:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:41 2008''