1joy: Difference between revisions

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

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

caption="1joy" />

'''SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.'''<br />

==Overview==

Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays, a central role in osmoregulation, a cellular adaptation process involving, the His-Asp phosphorelay signal transduction system. Dimerization of the, transmembrane protein is essential for its autophosphorylation and, phosphorelay signal transduction functions. Here we present the, NMR-derived structure of the homodimeric core domain (residues 223-289) of, EnvZ that includes His 243, the site of autophosphorylation and phosphate, transfer reactions. The structure comprises a four-helix bundle formed by, two identical helix-turn-helix subunits, revealing the molecular assembly, of two active sites within the dimeric kinase.

Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

==About this Structure==

1JOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1JOY OCA].

1JOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOY OCA].

==Reference==

Line 21:

[[Category: Park, H.]]

[[Category: Qian, H.]]

[[Category: Saha, S.K.]]

[[Category: Saha, S K.]]

[[Category: Tanaka, T.]]

[[Category: Tomomori, C.]]

[[Category: Tong, K.I.]]

[[Category: Tong, K I.]]

[[Category: Zhu, Y.]]

[[Category: histidine kinase]]

Line 32:

[[Category: sensory transduction]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 18~~:26:~~22 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:04 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1joy.jpg|left|200px]]<br /><applet load="1joy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1joy.jpg|left|200px]]<br /><applet load="1joy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1joy" />
 '''SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.'''<br />
 ==Overview==
-Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays, a central role in osmoregulation, a cellular adaptation process involving, the His-Asp phosphorelay signal transduction system. Dimerization of the, transmembrane protein is essential for its autophosphorylation and, phosphorelay signal transduction functions. Here we present the, NMR-derived structure of the homodimeric core domain (residues 223-289) of, EnvZ that includes His 243, the site of autophosphorylation and phosphate, transfer reactions. The structure comprises a four-helix bundle formed by, two identical helix-turn-helix subunits, revealing the molecular assembly, of two active sites within the dimeric kinase.
+Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.
 ==About this Structure==
-JOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JOY OCA].
+JOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOY OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: Park, H.]]
 [[Category: Qian, H.]]
-[[Category: Saha, S.K.]]
+[[Category: Saha, S K.]]
 [[Category: Tanaka, T.]]
 [[Category: Tomomori, C.]]
-[[Category: Tong, K.I.]]
+[[Category: Tong, K I.]]
 [[Category: Zhu, Y.]]
 [[Category: histidine kinase]]
@@ Line 32: / Line 32: @@
 [[Category: sensory transduction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:26:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:04 2008''