1xko: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
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|RELATEDENTRY=[[1squ|1SQU]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xko OCA], [http://www.ebi.ac.uk/pdbsum/1xko PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xko RCSB]</span>
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[[Category: signal transduction]]
[[Category: signal transduction]]


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Revision as of 00:51, 31 March 2008

File:1xko.jpg


PDB ID 1xko

Drag the structure with the mouse to rotate
, resolution 2.48Å
Related: 1SQU


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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