2chy: Difference between revisions

Revision as of 17:48, 21 February 2008

THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS

OverviewOverview

Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of the Salmonella typhimurium CheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.

About this StructureAbout this Structure

2CHY is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis., Stock AM, Mottonen JM, Stock JB, Schutt CE, Nature. 1989 Feb 23;337(6209):745-9. PMID:2645526

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OCA

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-[[Image:2chy.jpg|left|200px]]<br /><applet load="2chy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2chy.jpg|left|200px]]<br /><applet load="2chy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2chy, resolution 2.7&Aring;" />
 '''THREE-DIMENSIONAL STRUCTURE OF CHEY, THE RESPONSE REGULATOR OF BACTERIAL CHEMOTAXIS'''<br />
 ==Overview==
-Homologies among bacterial signal transduction proteins suggest that a, common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen, deprivation. A common kinase-mediated phosphotransfer reaction has, recently been identified in chemotaxis, nitrogen regulation, and, osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group, to the cytoplasmic protein CheY, which functions as a, phosphorylation-activated switch that interacts with flagellar components, to regulate motility. We report here the X-ray crystal structure of the, Salmonella typhimurium CheY protein. The determination of the structure, was facilitated by the use of site-specific mutagenesis to engineer, heavy-atom binding sites. CheY is a single-domain protein composed of a, doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site, in CheY is probably a cluster of aspartic-acid side chains near the, C-terminal edge of the beta-sheet. The pattern of sequence similarity of, CheY with components of other regulatory systems can be interpreted in the, light of the CheY structure and supports the view that this family of, proteins have a common structural motif and active site.
+Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of the Salmonella typhimurium CheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.
 ==About this Structure==
-CHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHY OCA].
+CHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHY OCA].
 ==Reference==
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 [[Category: Salmonella typhimurium]]
 [[Category: Single protein]]
-[[Category: Mottonen, J.M.]]
+[[Category: Mottonen, J M.]]
-[[Category: Schutt, C.E.]]
+[[Category: Schutt, C E.]]
-[[Category: Stock, A.M.]]
+[[Category: Stock, A M.]]
-[[Category: Stock, J.B.]]
+[[Category: Stock, J B.]]
 [[Category: signal transduction protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:07:45 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:58 2008''