1xko

Structure of Thermotoga maritima CheX

spinqualitylabelsall models 1xko, resolution 2.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xko is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.48Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHEX_THEMA Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. It has a greater activity than CheC. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures

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