1xko: Difference between revisions

Revision as of 16:55, 21 February 2008

Structure of Thermotoga maritima CheX

OverviewOverview

In bacterial chemotaxis, phosphorylated CheY levels control the sense of flagella rotation and thereby determine swimming behavior. In E. coli, CheY dephosphorylation by CheZ extinguishes the switching signal. But, instead of CheZ, many chemotactic bacteria contain CheC, CheD, and/or CheX. The crystal structures of T. maritima CheC and CheX reveal a common fold unlike that of any other known protein. Unlike CheC, CheX dimerizes via a continuous beta sheet between subunits. T. maritima CheC, as well as CheX, dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. Structural analyses identified one conserved active site in CheX and two in CheC; mutations therein reduce CheY-phosphatase activity, but only mutants of two invariant asparagine residues are completely inactive even in the presence of CheD. Our structures indicate that the flagellar switch components FliY and FliM resemble CheC more closely than CheX, but attribute phosphatase activity only to FliY.

About this StructureAbout this Structure

1XKO is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

ReferenceReference

Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX., Park SY, Chao X, Gonzalez-Bonet G, Beel BD, Bilwes AM, Crane BR, Mol Cell. 2004 Nov 19;16(4):563-74. PMID:15546616

Page seeded by OCA on Thu Feb 21 15:55:55 2008

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OCA

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-[[Image:1xko.jpg|left|200px]]<br /><applet load="1xko" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1xko.jpg|left|200px]]<br /><applet load="1xko" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1xko, resolution 2.48&Aring;" />
 '''Structure of Thermotoga maritima CheX'''<br />
 ==Overview==
-In bacterial chemotaxis, phosphorylated CheY levels control the sense of, flagella rotation and thereby determine swimming behavior. In E. coli, CheY dephosphorylation by CheZ extinguishes the switching signal. But, instead of CheZ, many chemotactic bacteria contain CheC, CheD, and/or, CheX. The crystal structures of T. maritima CheC and CheX reveal a common, fold unlike that of any other known protein. Unlike CheC, CheX dimerizes, via a continuous beta sheet between subunits. T. maritima CheC, as well as, CheX, dephosphorylate CheY, although CheC requires binding of CheD to, achieve the activity of CheX. Structural analyses identified one conserved, active site in CheX and two in CheC; mutations therein reduce, CheY-phosphatase activity, but only mutants of two invariant asparagine, residues are completely inactive even in the presence of CheD. Our, structures indicate that the flagellar switch components FliY and FliM, resemble CheC more closely than CheX, but attribute phosphatase activity, only to FliY.
+In bacterial chemotaxis, phosphorylated CheY levels control the sense of flagella rotation and thereby determine swimming behavior. In E. coli, CheY dephosphorylation by CheZ extinguishes the switching signal. But, instead of CheZ, many chemotactic bacteria contain CheC, CheD, and/or CheX. The crystal structures of T. maritima CheC and CheX reveal a common fold unlike that of any other known protein. Unlike CheC, CheX dimerizes via a continuous beta sheet between subunits. T. maritima CheC, as well as CheX, dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. Structural analyses identified one conserved active site in CheX and two in CheC; mutations therein reduce CheY-phosphatase activity, but only mutants of two invariant asparagine residues are completely inactive even in the presence of CheD. Our structures indicate that the flagellar switch components FliY and FliM resemble CheC more closely than CheX, but attribute phosphatase activity only to FliY.
 ==About this Structure==
-XKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XKO OCA].
+XKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKO OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Beel, B.D.]]
+[[Category: Beel, B D.]]
-[[Category: Bilwes, A.M.]]
+[[Category: Bilwes, A M.]]
 [[Category: Chao, X.]]
-[[Category: Crane, B.R.]]
+[[Category: Crane, B R.]]
 [[Category: Gonzalez-Bonet, G.]]
-[[Category: Park, S.Y.]]
+[[Category: Park, S Y.]]
 [[Category: chemotaxis]]
 [[Category: protein phosphatase]]
 [[Category: signal transduction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:07:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:55 2008''